| Year |
Citation |
Score |
| 2023 |
Zaragoza JPT, Offenbacher AR, Hu S, Gee CL, Firestein ZM, Minnetian N, Deng Z, Fan F, Iavarone AT, Klinman JP. Temporal and spatial resolution of distal protein motions that activate hydrogen tunneling in soybean lipoxygenase. Proceedings of the National Academy of Sciences of the United States of America. 120: e2211630120. PMID 36867685 DOI: 10.1073/pnas.2211630120 |
0.835 |
|
| 2022 |
Klinman JP. Dynamical activation of function in metalloenzymes. Febs Letters. PMID 36239559 DOI: 10.1002/1873-3468.14515 |
0.341 |
|
| 2022 |
Gao S, Zhang W, Barrow SL, Iavarone AT, Klinman JP. Temperature-dependent hydrogen deuterium exchange shows impact of analog binding on adenosine deaminase flexibility but not embedded thermal networks. The Journal of Biological Chemistry. 102350. PMID 35933011 DOI: 10.1016/j.jbc.2022.102350 |
0.79 |
|
| 2022 |
Gao S, Klinman JP. Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts. Current Opinion in Structural Biology. 75: 102434. PMID 35872562 DOI: 10.1016/j.sbi.2022.102434 |
0.794 |
|
| 2021 |
Gao S, Thompson EJ, Barrow SL, Zhang W, Iavarone AT, Klinman JP. Correction to "Hydrogen-Deuterium Exchange within Adenosine Deaminase, a TIM Barrel Hydrolase, Identifies Networks for Thermal Activation of Catalysis". Journal of the American Chemical Society. PMID 33570951 DOI: 10.1021/jacs.1c01046 |
0.787 |
|
| 2021 |
Thompson EJ, Paul A, Iavarone AT, Klinman JP. Identification of Thermal Conduits That Link the Protein-Water Interface to the Active Site Loop and Catalytic Base in Enolase. Journal of the American Chemical Society. PMID 33395523 DOI: 10.1021/jacs.0c09423 |
0.728 |
|
| 2020 |
Gao S, Thompson EJ, Barrow SL, Zhang W, Iavarone AT, Klinman JP. Hydrogen-Deuterium Exchange within Adenosine Deaminase, a TIM Barrel Hydrolase, Identifies Networks for Thermal Activation of Catalysis. Journal of the American Chemical Society. PMID 33181018 DOI: 10.1021/jacs.0c07866 |
0.832 |
|
| 2020 |
Zhu W, Klinman JP. Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone. Current Opinion in Chemical Biology. 59: 93-103. PMID 32731194 DOI: 10.1016/J.Cbpa.2020.05.001 |
0.455 |
|
| 2020 |
Zhu W, Walker LM, Tao L, Iavarone AT, Wei X, Britt RD, Elliott SJ, Klinman JP. Structural Properties and Catalytic Implications of the SPASM Domain Iron-Sulfur Clusters in PqqE. Journal of the American Chemical Society. PMID 32643933 DOI: 10.1021/Jacs.0C02044 |
0.509 |
|
| 2020 |
Zhang J, Balsbaugh JL, Gao S, Ahn NG, Klinman JP. Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catechol -methyltransferase reaction. Proceedings of the National Academy of Sciences of the United States of America. PMID 32371482 DOI: 10.1073/Pnas.1917219117 |
0.84 |
|
| 2020 |
Offenbacher AR, Sharma A, Doan PE, Klinman JP, Hoffman BM. The Soybean Lipoxygenase-Substrate Complex: Correlation between the Properties of Tunneling-Ready States and ENDOR-Detected Structures of Ground States. Biochemistry. PMID 32022556 DOI: 10.1021/Acs.Biochem.9B00861 |
0.771 |
|
| 2019 |
Tao L, Zhu W, Klinman JP, Britt RD. EPR Spectroscopic Identification of the Fe-S Clusters in the SPASM-Domain Containing Radical SAM Enzyme PqqE. Biochemistry. PMID 31769977 DOI: 10.1021/Acs.Biochem.9B00960 |
0.455 |
|
| 2019 |
Hu S, Offenbacher AR, Lu ED, Klinman JP. Comparative kinetic isotope effects on first- and second-order rate constants of soybean lipoxygenase variants uncover a substrate-binding network. The Journal of Biological Chemistry. PMID 31624150 DOI: 10.1074/Jbc.Ra119.010826 |
0.828 |
|
| 2019 |
Zaragoza JPT, Nguy A, Minnetian N, Deng Z, Iavarone AT, Offenbacher AR, Klinman JP. Detecting and Characterizing the Kinetic Activation of Thermal Networks in Proteins: Thermal Transfer from a Distal, Solvent-Exposed Loop to the Active Site in Soybean Lipoxygenase. The Journal of Physical Chemistry. B. PMID 31580070 DOI: 10.1021/Acs.Jpcb.9B07228 |
0.821 |
|
| 2019 |
Martins AM, Latham JA, Martel PJ, Barr I, Iavarone AT, Klinman JP. A two-component protease in with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone. The Journal of Biological Chemistry. PMID 31427437 DOI: 10.1074/Jbc.Ra119.009684 |
0.584 |
|
| 2019 |
Masson GR, Burke JE, Ahn NG, Anand GS, Borchers C, Brier S, Bou-Assaf GM, Engen JR, Englander SW, Faber J, Garlish R, Griffin PR, Gross ML, Guttman M, Hamuro Y, ... ... Klinman JP, et al. Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments. Nature Methods. 16: 595-602. PMID 31249422 DOI: 10.1038/S41592-019-0459-Y |
0.542 |
|
| 2019 |
Klinman JP. Moving Through Barriers in Science and Life. Annual Review of Biochemistry. 88: 1-24. PMID 31220975 DOI: 10.1146/Annurev-Biochem-013118-111217 |
0.318 |
|
| 2019 |
Koehn EM, Latham JA, Armand T, Evans RL, Tu X, Wilmot CM, Iavarone AT, Klinman JP. Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway. Journal of the American Chemical Society. PMID 30811189 DOI: 10.1021/Jacs.8B13453 |
0.779 |
|
| 2019 |
Hu S, Offenbacher AR, Thompson EM, Gee CL, Wilcoxen J, Carr CAM, Prigozhin DM, Yang V, Alber T, Britt RD, Fraser JS, Klinman JP. Biophysical Characterization of a Disabled Double Mutant of Soybean Lipoxygenase: The "Undoing" of Precise Substrate Positioning Relative to Metal Cofactor and an Identified Dynamical Network. Journal of the American Chemical Society. PMID 30645119 DOI: 10.1021/Jacs.8B10992 |
0.831 |
|
| 2018 |
Klinman JP, Offenbacher AR. Understanding Biological Hydrogen Transfer Through the Lens of Temperature Dependent Kinetic Isotope Effects. Accounts of Chemical Research. PMID 30152685 DOI: 10.1021/Acs.Accounts.8B00226 |
0.769 |
|
| 2018 |
Zhu W, Martins AM, Klinman JP. Methods for Expression, Purification, and Characterization of PqqE, a Radical SAM Enzyme in the PQQ Biosynthetic Pathway. Methods in Enzymology. 606: 389-420. PMID 30097100 DOI: 10.1016/Bs.Mie.2018.04.002 |
0.535 |
|
| 2018 |
Barr I, Stich TA, Gizzi AS, Grove TL, Bonanno JB, Latham JA, Chung T, Wilmot CM, Britt RD, Almo SC, Klinman JP. X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE. Biochemistry. PMID 29405700 DOI: 10.1021/Acs.Biochem.7B01097 |
0.541 |
|
| 2018 |
Vaughn MB, Zhang J, Spiro TG, Dyer RB, Klinman JP. Activity-Related Microsecond Dynamics Revealed by Temperature-Jump Förster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase. Journal of the American Chemical Society. PMID 29323490 DOI: 10.1021/Jacs.7B12369 |
0.47 |
|
| 2017 |
Hu S, Soudackov AV, Hammes-Schiffer S, Klinman JP. Enhanced Rigidification within a Double Mutant of Soybean Lipoxygenase Provides Experimental Support for Vibronically Nonadiabatic Proton-Coupled Electron Transfer Models. Acs Catalysis. 7: 3569-3574. PMID 29250456 DOI: 10.1021/Acscatal.7B00688 |
0.814 |
|
| 2017 |
Klinman JP, Offenbacher AR, Hu S. Origins of Enzyme Catalysis: Experimental Findings for C-H Activation, New Models, and Their Relevance to Prevailing Theoretical Constructs. Journal of the American Chemical Society. PMID 29244501 DOI: 10.1021/Jacs.7B08418 |
0.823 |
|
| 2017 |
Offenbacher AR, Iavarone AT, Klinman JP. Hydrogen-deuterium exchange reveals long-range dynamical allostery in soybean lipoxygenase. The Journal of Biological Chemistry. PMID 29191828 DOI: 10.1074/Jbc.M117.817197 |
0.734 |
|
| 2017 |
Latham JA, Barr I, Klinman JP. At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology. The Journal of Biological Chemistry. PMID 28830931 DOI: 10.1074/Jbc.R117.797399 |
0.583 |
|
| 2017 |
Tu X, Latham JA, Klema VJ, Evans RL, Li C, Klinman JP, Wilmot CM. Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 28825148 DOI: 10.1007/S00775-017-1486-8 |
0.32 |
|
| 2017 |
Offenbacher AR, Hu S, Poss EM, Carr CAM, Scouras AD, Prigozhin DM, Iavarone AT, Palla A, Alber T, Fraser JS, Klinman JP. Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling. Acs Central Science. 3: 570-579. PMID 28691068 DOI: 10.1021/Acscentsci.7B00142 |
0.837 |
|
| 2017 |
Evans RL, Latham JA, Xia Y, Klinman JP, Wilmot CM. NMR structure and binding studies of PqqD, a chaperone required in the biosynthesis of the bacterial dehydrogenase cofactor pyrroloquinoline quinone. Biochemistry. PMID 28481092 DOI: 10.1021/Acs.Biochem.7B00247 |
0.354 |
|
| 2017 |
Horitani M, Offenbacher AR, Carr CA, Yu T, Hoeke V, Cutsail GE, Hammes-Schiffer S, Klinman JP, Hoffman BM. (13)C ENDOR Spectroscopy of Lipoxygenase-Substrate Complexes Reveals the Structural Basis for C-H Activation by Tunneling. Journal of the American Chemical Society. PMID 28121140 DOI: 10.1021/Jacs.6B11856 |
0.828 |
|
| 2016 |
Offenbacher AR, Zhu H, Klinman JP. Synthesis of Site-Specifically (13)C Labeled Linoleic Acids. Tetrahedron Letters. 57: 4537-4540. PMID 28260819 DOI: 10.1016/J.Tetlet.2016.08.071 |
0.712 |
|
| 2016 |
Kulik HJ, Zhang J, Klinman JP, Martínez TJ. How Large Should the QM Region Be in QM/MM Calculations? The Case of Catechol O-methyltransferase. The Journal of Physical Chemistry. B. PMID 27704827 DOI: 10.1021/Acs.Jpcb.6B07814 |
0.389 |
|
| 2016 |
Evans RL, Latham JA, Klinman JP, Wilmot CM, Xia Y. (1)H, (13)C, and (15)N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA. Biomolecular Nmr Assignments. PMID 27638737 DOI: 10.1007/S12104-016-9705-8 |
0.385 |
|
| 2016 |
Zhang J, Klinman JP. Convergent Mechanistic Features Between the Structurally Diverse N- and O-Methyltransferases: Glycine N-Methyltransferase and Catechol O- Methyltransferase. Journal of the American Chemical Society. PMID 27355841 DOI: 10.1021/Jacs.6B03462 |
0.396 |
|
| 2016 |
Hu S, Cattin-Ortolá J, Munos JW, Klinman JP. Hydrostatic Pressure Studies Distinguish Global from Local Protein Motions in C-H Activation by Soybean Lipoxygenase-1. Angewandte Chemie (International Ed. in English). PMID 27348724 DOI: 10.1002/Anie.201603592 |
0.802 |
|
| 2016 |
Barr I, Latham JA, Iavarone AT, Chantarojsiri T, Hwang JD, Klinman JP. The pyrroloquinoline quinone (PQQ) biosynthetic pathway: Demonstration of de novo carbon-carbon cross-linking within the peptide substrate (PqqA) in the presence of the Radical SAM enzyme (PqqE) and its peptide chaperone (PqqD). The Journal of Biological Chemistry. PMID 26961875 DOI: 10.1074/Jbc.C115.699918 |
0.574 |
|
| 2016 |
Collazo L, Klinman JP. Control of the Position of Oxygen Delivery in Soybean Lipoxygenase-1 by Amino Acid Side Chains within a Gas Migration Channel. The Journal of Biological Chemistry. PMID 26867580 DOI: 10.1074/Jbc.M115.709154 |
0.416 |
|
| 2016 |
Offenbacher AR, Zhu H, Klinman JP. Synthesis of site-specifically 13C labeled linoleic acids Tetrahedron Letters. 57: 4537-4540. DOI: 10.1016/j.tetlet.2016.08.071 |
0.68 |
|
| 2015 |
Klinman JP. Low Barrier Hydrogen Bonds: Getting Close, but Not Sharing... Acs Central Science. 1: 115-6. PMID 27162960 DOI: 10.1021/Acscentsci.5B00215 |
0.361 |
|
| 2015 |
Zhu H, Peck SC, Bonnot F, van der Donk WA, Klinman JP. Oxygen-18 Kinetic Isotope Effects of Nonheme Iron Enzymes HEPD and MPnS Support Iron(III) Superoxide as the Hydrogen Abstraction Species. Journal of the American Chemical Society. PMID 26267117 DOI: 10.1021/Jacs.5B03907 |
0.386 |
|
| 2015 |
Meadows CW, Balakrishnan G, Kier BL, Spiro TG, Klinman JP. Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase. Journal of the American Chemical Society. PMID 26223665 DOI: 10.1021/Jacs.5B04413 |
0.781 |
|
| 2015 |
Sharma SC, Klinman JP. Kinetic Detection of Orthogonal Protein and Chemical Coordinates in Enzyme Catalysis: Double Mutants of Soybean Lipoxygenase. Biochemistry. PMID 26154975 DOI: 10.1021/Acs.Biochem.5B00374 |
0.502 |
|
| 2015 |
Zhang J, Kulik HJ, Martinez TJ, Klinman JP. Mediation of donor-acceptor distance in an enzymatic methyl transfer reaction. Proceedings of the National Academy of Sciences of the United States of America. 112: 7954-9. PMID 26080432 DOI: 10.1073/Pnas.1506792112 |
0.463 |
|
| 2015 |
Zhu H, Sommerhalter M, Nguy AK, Klinman JP. Solvent and Temperature Probes of the Long-Range Electron-Transfer Step in Tyramine β-Monooxygenase: Demonstration of a Long-Range Proton-Coupled Electron-Transfer Mechanism. Journal of the American Chemical Society. 137: 5720-9. PMID 25919134 DOI: 10.1021/Ja512388N |
0.79 |
|
| 2015 |
Hammes-Schiffer S, Klinman J. Emerging concepts about the role of protein motion in enzyme catalysis. Accounts of Chemical Research. 48: 899. PMID 25896141 DOI: 10.1021/Acs.Accounts.5B00113 |
0.37 |
|
| 2015 |
Latham JA, Iavarone AT, Barr I, Juthani PV, Klinman JP. PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway. The Journal of Biological Chemistry. 290: 12908-18. PMID 25817994 DOI: 10.1074/Jbc.M115.646521 |
0.561 |
|
| 2015 |
Klinman JP. Dynamically achieved active site precision in enzyme catalysis. Accounts of Chemical Research. 48: 449-56. PMID 25539048 DOI: 10.1021/Ar5003347 |
0.489 |
|
| 2014 |
Meadows CW, Tsang JE, Klinman JP. Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication. Journal of the American Chemical Society. 136: 14821-33. PMID 25314615 DOI: 10.1021/Ja506667K |
0.81 |
|
| 2014 |
Klinman JP, Kohen A. Evolutionary aspects of enzyme dynamics. The Journal of Biological Chemistry. 289: 30205-12. PMID 25210031 DOI: 10.1074/Jbc.R114.565515 |
0.731 |
|
| 2014 |
Meadows CW, Ou R, Klinman JP. Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis. The Journal of Physical Chemistry. B. 118: 6049-61. PMID 24892947 DOI: 10.1021/Jp500825X |
0.802 |
|
| 2014 |
Hu S, Sharma SC, Scouras AD, Soudackov AV, Carr CA, Hammes-Schiffer S, Alber T, Klinman JP. Extremely elevated room-temperature kinetic isotope effects quantify the critical role of barrier width in enzymatic C-H activation. Journal of the American Chemical Society. 136: 8157-60. PMID 24884374 DOI: 10.1021/Ja502726S |
0.833 |
|
| 2014 |
Carr CAM, Klinman JP. Hydrogen tunneling in a prokaryotic lipoxygenase Biochemistry. 53: 2212-2214. PMID 24641705 DOI: 10.1021/Bi500070Q |
0.427 |
|
| 2014 |
Klinman JP, Bonnot F. Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ Chemical Reviews. 114: 4343-4365. PMID 24350630 DOI: 10.1021/Cr400475G |
0.365 |
|
| 2014 |
Klinman JP. The power of integrating kinetic isotope effects into the formalism of the Michaelis-Menten equation Febs Journal. 281: 489-497. PMID 23937475 DOI: 10.1111/Febs.12477 |
0.41 |
|
| 2014 |
Klinman JP, Kohen A. Evolutionary aspects of enzyme dynamics Journal of Biological Chemistry. 289: 30205-30212. DOI: 10.1074/jbc.R114.565515 |
0.67 |
|
| 2014 |
Meadows CW, Ou R, Klinman JP. Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: Relationship of temperature-dependent changes in fluorescence to catalysis Journal of Physical Chemistry B. 118: 6049-6061. DOI: 10.1021/jp500825x |
0.752 |
|
| 2014 |
Meadows CW, Tsang JE, Klinman JP. Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication Journal of the American Chemical Society. 136: 14821-14833. DOI: 10.1021/ja506667k |
0.76 |
|
| 2014 |
Meadows CW, Klinman JP. Modulation of Active Site Picosecond Dynamics in Mutant Forms of a Thermophilic Alcohol Dehydrogenase (HT-ADH) Biophysical Journal. 106: 648a. DOI: 10.1016/J.Bpj.2013.11.3588 |
0.797 |
|
| 2013 |
Johnson BJ, Yukl ET, Klema VJ, Klinman JP, Wilmot CM. Structural snapshots from the oxidative half-reaction of a copper amine oxidase: Implications for O2 activation Journal of Biological Chemistry. 288: 28409-28417. PMID 23940035 DOI: 10.1074/Jbc.M113.501791 |
0.383 |
|
| 2013 |
Klinman JP, Kohen A. Hydrogen tunneling links protein dynamics to enzyme catalysis Annual Review of Biochemistry. 82: 471-496. PMID 23746260 DOI: 10.1146/Annurev-Biochem-051710-133623 |
0.744 |
|
| 2013 |
Bonnot F, Iavarone AT, Klinman JP. Multistep, eight-electron oxidation catalyzed by the cofactorless oxidase, PqqC: Identification of chemical intermediates and their dependence on molecular oxygen Biochemistry. 52: 4667-4675. PMID 23718207 DOI: 10.1021/Bi4003315 |
0.393 |
|
| 2013 |
Nagel ZD, Cun S, Klinman JP. Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases Journal of Biological Chemistry. 288: 14087-14097. PMID 23525111 DOI: 10.1074/Jbc.M113.453951 |
0.726 |
|
| 2013 |
Klema VJ, Solheid CJ, Klinman JP, Wilmot CM. Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from hansenula polymorpha Biochemistry. 52: 2291-2301. PMID 23452079 DOI: 10.1021/Bi3016845 |
0.444 |
|
| 2013 |
Klinman JP. Importance of protein dynamics during enzymatic C-H bond cleavage catalysis Biochemistry. 52: 2068-2077. PMID 23373460 DOI: 10.1021/Bi301504M |
0.401 |
|
| 2013 |
Osborne RL, Zhu H, Iavarone AT, Blackburn NJ, Klinman JP. Interdomain long-range electron transfer becomes rate-limiting in the Y216A variant of tyramine β-monooxygenase Biochemistry. 52: 1179-1191. PMID 23320946 DOI: 10.1021/Bi3013609 |
0.343 |
|
| 2013 |
Johnson BJ, Yukl ET, Klema VJ, Klinman JP, Wilmot CM. Structural evidence for the semiquinone in a copper amine oxidase from Hansenula polymorpha: implications for the catalytic mechanism Journal of Biological Chemistry. DOI: 10.2210/Pdb4Kfd/Pdb |
0.333 |
|
| 2012 |
Osborne RL, Zhu H, Iavarone AT, Hess CR, Klinman JP. Inactivation of Met471Cys tyramine β-monooxygenase results from site-specific cysteic acid formation Biochemistry. 51: 7488-7495. PMID 22891760 DOI: 10.1021/Bi300456F |
0.326 |
|
| 2012 |
Klema VJ, Johnson BJ, Klinman JP, Wilmot CM. The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with Cu I and Co II Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 68: 501-510. PMID 22691777 DOI: 10.1107/S1744309112012857 |
0.336 |
|
| 2012 |
Nagel ZD, Meadows CW, Dong M, Bahnson BJ, Klinman JP. Active site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures Biochemistry. 51: 4147-4156. PMID 22568562 DOI: 10.1021/Bi3001352 |
0.825 |
|
| 2012 |
Shen YQ, Bonnot F, Imsand EM, RoseFigura JM, Sjölander K, Klinman JP. Distribution and properties of the genes encoding the biosynthesis of the bacterial cofactor, pyrroloquinoline quinone. Biochemistry. 51: 2265-75. PMID 22324760 DOI: 10.1021/Bi201763D |
0.778 |
|
| 2012 |
Shen SH, Wertz DL, Klinman JP. Implication for functions of the ectopic adipocyte copper amine oxidase (AOC3) from purified enzyme and cell-based kinetic studies Plos One. 7. PMID 22238597 DOI: 10.1371/Journal.Pone.0029270 |
0.632 |
|
| 2011 |
Zhang J, Klinman JP. Enzymatic methyl transfer: Role of an active site residue in generating active site compaction that correlates with catalytic efficiency Journal of the American Chemical Society. 133: 17134-17137. PMID 21958159 DOI: 10.1021/Ja207467D |
0.444 |
|
| 2011 |
Oyeyemi OA, Sours KM, Lee T, Kohen A, Resing KA, Ahn NG, Klinman JP. Comparative hydrogen-deuterium exchange for a mesophilic vs thermophilic dihydrofolate reductase at 25 °c: Identification of a single active site region with enhanced flexibility in the mesophilic protein Biochemistry. 50: 8251-8260. PMID 21859100 DOI: 10.1021/Bi200640S |
0.809 |
|
| 2011 |
Nagel ZD, Dong M, Bahnson BJ, Klinman JP. Impaired protein conformational landscapes as revealed in anomalous Arrhenius prefactors Proceedings of the National Academy of Sciences of the United States of America. 108: 10520-10525. PMID 21670258 DOI: 10.1073/Pnas.1104989108 |
0.826 |
|
| 2011 |
Meyer MP, Klinman JP. Investigating inner-sphere reorganization via secondary kinetic isotope effects in the C-H cleavage reaction catalyzed by soybean lipoxygenase: tunneling in the substrate backbone as well as the transferred hydrogen. Journal of the American Chemical Society. 133: 430-9. PMID 21192631 DOI: 10.1021/Ja1050742 |
0.693 |
|
| 2011 |
RoseFigura JM, Ehringer S, Schwarzenbacher R, Toyama H, Klinman JP. Characterization of a protein-generated O 2 binding pocket in PqqC, a cofactorless oxidase catalyzing the final step in PQQ production Biochemistry. 50: 1556-1566. PMID 21155540 DOI: 10.1021/Bi1015474 |
0.807 |
|
| 2011 |
Klinman JP. The widespread occurrence of enzymatic hydrogen tunneling, and its unique properties, lead to a new physical model for the origins of enzyme catalysis Procedia Chemistry. 3: 291-305. DOI: 10.1016/J.Proche.2011.08.037 |
0.465 |
|
| 2010 |
Nagel ZD, Klinman JP. Update 1 of: Tunneling and dynamics in enzymatic hydride transfer. Chemical Reviews. 110: PR41-67. PMID 21141912 DOI: 10.1021/Cr1001035 |
0.743 |
|
| 2010 |
Klinman JP. Enzyme dynamics: Control of active-site compression Nature Chemistry. 2: 907-909. PMID 20966941 DOI: 10.1038/Nchem.886 |
0.433 |
|
| 2010 |
Chen ZW, Datta S, Dubois JL, Klinman JP, Mathews FS. Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity. Biochemistry. 49: 7393-402. PMID 20684524 DOI: 10.1021/Bi100643Y |
0.653 |
|
| 2010 |
Puehringer S, Rosefigura J, Metlitzky M, Toyama H, Klinman JP, Schwarzenbacher R. Structural studies of mutant forms of the PQQ-forming enzyme PqqC in the presence of product and substrate Proteins: Structure, Function and Bioinformatics. 78: 2554-2562. PMID 20602352 DOI: 10.1002/Prot.22769 |
0.825 |
|
| 2010 |
Oyeyemi OA, Sours KM, Lee T, Resing KA, Ahn NG, Klinman JP. Temperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency Proceedings of the National Academy of Sciences of the United States of America. 107: 10074-10079. PMID 20534574 DOI: 10.1073/Pnas.1003678107 |
0.82 |
|
| 2010 |
Gleick PH, Adams RM, Amasino RM, Anders E, Anderson DJ, Anderson WW, Anselin LE, Arroyo MK, Asfaw B, Ayala FJ, Bax A, Bebbington AJ, Bell G, Bennett MV, Bennetzen JL, ... ... Klinman JP, et al. Climate change and the integrity of science. Science (New York, N.Y.). 328: 689-90. PMID 20448167 DOI: 10.1126/Science.328.5979.689 |
0.337 |
|
| 2010 |
McCusker KP, Klinman JP. An active-site phenylalanine directs substrate binding and C-H cleavage in the α-ketoglutarate-dependent dioxygenase AauD Journal of the American Chemical Society. 132: 5114-5120. PMID 20302299 DOI: 10.1021/Ja909416Z |
0.791 |
|
| 2010 |
Chang CM, Klema VJ, Johnson BJ, Mure M, Klinman JP, Wilmot CM. Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha Biochemistry. 49: 2540-2550. PMID 20155950 DOI: 10.1021/Bi901933D |
0.622 |
|
| 2010 |
Nagel ZD, Klinman JP. Update 1 of: Tunneling and dynamics in enzymatic hydride transfer Chemical Reviews. 110: PR41-PR67. DOI: 10.1021/cr1001035 |
0.648 |
|
| 2010 |
Klinman JP. A new model for the origin of kinetic hydrogen isotope effects Journal of Physical Organic Chemistry. 23: 606-612. DOI: 10.1002/Poc.1661 |
0.339 |
|
| 2009 |
Klinman JP. An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling. Chemical Physics Letters. 471: 179-193. PMID 20354595 DOI: 10.1016/J.Cplett.2009.01.038 |
0.487 |
|
| 2009 |
McCusker KP, Klinman JP. Modular behavior of tauD provides insight into the origin of specificity in α-ketoglutarate-dependent nonheme iron oxygenases Proceedings of the National Academy of Sciences of the United States of America. 106: 19791-19795. PMID 19892731 DOI: 10.1073/Pnas.0910660106 |
0.772 |
|
| 2009 |
Wecksler SR, Stoll S, Tran H, Magnusson OT, Wu SP, King D, Britt RD, Klinman JP. Pyrroloquinoline quinone biogenesis: Demonstration that PqqE from Klebsiella pneumoniae is a radical S-adenosyl-L-methionine enzyme Biochemistry. 48: 10151-10161. PMID 19746930 DOI: 10.1021/Bi900918B |
0.421 |
|
| 2009 |
Nagel ZD, Klinman JP. A 21st century revisionist's view at a turning point in enzymology. Nature Chemical Biology. 5: 543-50. PMID 19620995 DOI: 10.1038/Nchembio.204 |
0.735 |
|
| 2009 |
Humphreys KJ, Mirica LM, Wang Y, Klinman JP. Galactose oxidase as a model for reactivity at a copper superoxide center. Journal of the American Chemical Society. 131: 4657-63. PMID 19290629 DOI: 10.1021/Ja807963E |
0.798 |
|
| 2009 |
Nagel ZD, Klinman JP. A 21st century revisionist's view at a turning point in enzymology (Nature Chemical Biology (2009) 5, (543-550)) Nature Chemical Biology. 5: 696. DOI: 10.1038/Nchembio0909-696C |
0.634 |
|
| 2009 |
McCusker KP, Klinman JP. Facile synthesis of 1,1-[2H2]-2-methylaminoethane-1-sulfonic acid as a substrate for taurine α ketoglutarate dioxygenase (TauD) Tetrahedron Letters. 50: 611-613. DOI: 10.1016/J.Tetlet.2008.11.063 |
0.723 |
|
| 2008 |
Meyer MP, Klinman JP. Synthesis of linoleic acids combinatorially-labeled at the vinylic positions as substrates for lipoxygenases. Tetrahedron Letters. 49: 3600-3603. PMID 19543446 DOI: 10.1016/J.Tetlet.2008.04.023 |
0.67 |
|
| 2008 |
Sharma SC, Klinman JP. Experimental evidence for hydrogen tunneling when the isotopic arrhenius prefactor (A h/A d) is unity Journal of the American Chemical Society. 130: 17632-17633. PMID 19061319 DOI: 10.1021/Ja806354W |
0.396 |
|
| 2008 |
Hess CR, Wu Z, Ng A, Gray EE, McGuirl MA, Klinman JP. Hydroxylase activity of Met471Cys tyramine beta-monooxygenase. Journal of the American Chemical Society. 130: 11939-44. PMID 18710228 DOI: 10.1021/Ja800408H |
0.403 |
|
| 2008 |
Mirica LM, McCusker KP, Munos JW, Liu HW, Klinman JP. 18O kinetic isotope effects in non-heme iron enzymes: probing the nature of Fe/O2 intermediates. Journal of the American Chemical Society. 130: 8122-3. PMID 18540575 DOI: 10.1021/Ja800265S |
0.781 |
|
| 2008 |
Mirica LM, Klinman JP. The nature of O2 activation by the ethylene-forming enzyme 1-aminocyclopropane-1-carboxylic acid oxidase. Proceedings of the National Academy of Sciences of the United States of America. 105: 1814-9. PMID 18238897 DOI: 10.1073/Pnas.0711626105 |
0.663 |
|
| 2008 |
Meyer MP, Tomchick DR, Klinman JP. Enzyme structure and dynamics affect hydrogen tunneling: the impact of a remote side chain (I553) in soybean lipoxygenase-1. Proceedings of the National Academy of Sciences of the United States of America. 105: 1146-51. PMID 18216254 DOI: 10.1073/Pnas.0710643105 |
0.723 |
|
| 2008 |
Hess CR, McGuirl MM, Klinman JP. Mechanism of the insect enzyme, tyramine beta-monooxygenase, reveals differences from the mammalian enzyme, dopamine beta-monooxygenase. The Journal of Biological Chemistry. 283: 3042-9. PMID 18032384 DOI: 10.1074/Jbc.M705911200 |
0.393 |
|
| 2008 |
Meyer MP, Tomchick DR, Klinman JP. Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1 (Proceedings of the National Academy of Sciences of the United States of America (2008) 105, 4, (1146-1151) DOI:10.1073/pnas.0710643105) Proceedings of the National Academy of Sciences of the United States of America. 105: 19562. DOI: 10.1073/Pnas.0809757105 |
0.35 |
|
| 2007 |
Welford RW, Lam A, Mirica LM, Klinman JP. Partial conversion of Hansenula polymorpha amine oxidase into a "plant" amine oxidase: implications for copper chemistry and mechanism. Biochemistry. 46: 10817-27. PMID 17760423 DOI: 10.1021/Bi700943R |
0.652 |
|
| 2007 |
Magnusson OT, Rosefigura JM, Toyama H, Schwarzenbacher R, Klinman JP. Pyrroloquinoline quinone biogenesis: Characterization of PqqC and its H84N and H84A active site variants Biochemistry. 46: 7174-7186. PMID 17523676 DOI: 10.1021/Bi700162N |
0.813 |
|
| 2007 |
Klinman JP. How do enzymes activate oxygen without inactivating themselves? Accounts of Chemical Research. 40: 325-33. PMID 17474709 DOI: 10.1021/Ar6000507 |
0.415 |
|
| 2007 |
Johnson BJ, Cohen J, Welford RW, Pearson AR, Schulten K, Klinman JP, Wilmot CM. Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase Journal of Biological Chemistry. 282: 17767-17776. PMID 17409383 DOI: 10.1074/Jbc.M701308200 |
0.444 |
|
| 2007 |
Knapp MJ, Meyer M, Klinman JP. Nuclear Tunneling in the Condensed Phase: Hydrogen Transfer in Enzyme Reactions Hydrogen-Transfer Reactions. 4: 1241-1284. DOI: 10.1002/9783527611546.ch39 |
0.499 |
|
| 2006 |
Purdy MM, Koo LS, Ortiz De Montellano PR, Klinman JP. Mechanism of O2 activation by cytochrome P450cam studied by isotope effects and transient state kinetics Biochemistry. 45: 15793-15806. PMID 17176102 DOI: 10.1021/Bi061726W |
0.715 |
|
| 2006 |
Thrower J, Mirica LM, McCusker KP, Klinman JP. Mechanistic investigations of 1-aminocyclopropane 1-carboxylic acid oxidase with alternate cyclic and acyclic substrates. Biochemistry. 45: 13108-17. PMID 17059228 DOI: 10.1021/Bi061097Q |
0.806 |
|
| 2006 |
Nagel ZD, Klinman JP. Tunneling and dynamics in enzymatic hydride transfer Chemical Reviews. 106: 3095-3118. PMID 16895320 DOI: 10.1021/Cr050301X |
0.73 |
|
| 2006 |
Klinman JP. Linking protein structure and dynamics to catalysis: The role of hydrogen tunnelling Philosophical Transactions of the Royal Society B: Biological Sciences. 361: 1323-1331. PMID 16873120 DOI: 10.1098/Rstb.2006.1870 |
0.472 |
|
| 2006 |
Samuels NM, Klinman JP. Investigation of cu(I)-dependent 2,4,5-trihydroxyphenylalanine quinone biogenesis in Hansenula polymorpha amine oxidase Journal of Biological Chemistry. 281: 21114-21118. PMID 16717088 DOI: 10.1074/Jbc.M601501200 |
0.323 |
|
| 2006 |
Takahashi K, Klinman JP. Relationship of stopped flow to steady state parameters in the dimeric copper amine oxidase from Hansenula polymorpha and the role of zinc in inhibiting activity at alternate copper-containing subunits Biochemistry. 45: 4683-4694. PMID 16584203 DOI: 10.1021/Bi0521893 |
0.452 |
|
| 2006 |
Klinman JP. The role of tunneling in enzyme catalysis of C-H activation Biochimica Et Biophysica Acta - Bioenergetics. 1757: 981-987. PMID 16546116 DOI: 10.1016/J.Bbabio.2005.12.004 |
0.467 |
|
| 2006 |
DuBois JL, Klinman JP. Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha. Biochemistry. 45: 3178-88. PMID 16519513 DOI: 10.1021/Bi052025M |
0.642 |
|
| 2006 |
Klinman JP. The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation Journal of Biological Chemistry. 281: 3013-3016. PMID 16301310 DOI: 10.1074/Jbc.R500011200 |
0.32 |
|
| 2006 |
Liang Z, Tsigos I, Bouriotis aV, Klinman JP. Impact of Protein Flexibility on Hydride-Transfer Parameters in Thermophilic and Psychrophilic Alcohol Dehydrogenases [J. Am. Chem. Soc. 2004, 126, 9500−9501]. Journal of the American Chemical Society. 128: 3467-3467. DOI: 10.1021/Ja069955T |
0.519 |
|
| 2005 |
Meyer MP, Klinman JP. Modeling temperature dependent kinetic isotope effects for hydrogen transfer in a series of soybean lipoxygenase mutants: The effect of anharmonicity upon transfer distance. Chemical Physics. 319: 283-296. PMID 21132078 DOI: 10.1016/J.Chemphys.2005.05.017 |
0.714 |
|
| 2005 |
Samuels NM, Klinman JP. 2,4,5-Trihydroxyphenylalanine quinone biogenesis in the copper amine oxidase from Hansenula polymorpha with the alternate metal nickel Biochemistry. 44: 14308-14317. PMID 16245947 DOI: 10.1021/Bi051176M |
0.361 |
|
| 2005 |
Kim HS, Damo SM, Lee SY, Wemmer D, Klinman JP. Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues. Biochemistry. 44: 11428-39. PMID 16114879 DOI: 10.1021/Bi050630J |
0.473 |
|
| 2005 |
DuBois JL, Klinman JP. The nature of O2 reactivity leading to topa quinone in the copper amine oxidase from Hansenula polymorpha and its relationship to catalytic turnover. Biochemistry. 44: 11381-8. PMID 16114875 DOI: 10.1021/Bi0504759 |
0.611 |
|
| 2005 |
Dubois JL, Klinman JP. Mechanism of post-translational quinone formation in copper amine oxidases and its relationship to the catalytic turnover. Archives of Biochemistry and Biophysics. 433: 255-65. PMID 15581581 DOI: 10.1016/J.Abb.2004.08.036 |
0.66 |
|
| 2005 |
Roth JP, Wincek R, Nodet G, Edmondson DE, McIntire aWS, Klinman JP. Oxygen Isotope Effects on Electron Transfer to O2 Probed Using Chemically Modified Flavins Bound to Glucose Oxidase [J. Am. Chem. Soc. 2004, 126, 15120−15131]. Journal of the American Chemical Society. 127: 5727-5727. DOI: 10.1021/Ja059904G |
0.617 |
|
| 2004 |
Liang ZX, Klinman JP. Structural bases of hydrogen tunneling in enzymes: Progress and puzzles Current Opinion in Structural Biology. 14: 648-655. PMID 15582387 DOI: 10.1016/J.Sbi.2004.10.008 |
0.624 |
|
| 2004 |
Roth JP, Wincek R, Nodet G, Edmondson DE, McIntire WS, Klinman JP. Oxygen isotope effects on electron transfer to O2 probed using chemically modified flavins bound to glucose oxidase. Journal of the American Chemical Society. 126: 15120-31. PMID 15548009 DOI: 10.1021/Ja047050E |
0.665 |
|
| 2004 |
Liang ZX, Tsigos I, Lee T, Bouriotis V, Resing KA, Ahn NG, Klinman JP. Evidence for increased local flexibility in psychrophilic alcohol dehydrogenase relative to its thermophilic homologue Biochemistry. 43: 14676-14683. PMID 15544338 DOI: 10.1021/Bi049004X |
0.714 |
|
| 2004 |
Francisco WA, Wille G, Smith AJ, Merkler DJ, Klinman JP. Investigation of the pathway for inter-copper electron transfer in peptidylglycine α-amidating monooxygenase Journal of the American Chemical Society. 126: 13168-13169. PMID 15479039 DOI: 10.1021/Ja046888Z |
0.317 |
|
| 2004 |
Liang ZX, Tsigos I, Bouriotis V, Klinman JP. Impact of protein flexibility on hydride-transfer parameters in thermophilic and psychrophilic alcohol dehydrogenases Journal of the American Chemical Society. 126: 9500-9501. PMID 15291528 DOI: 10.1021/Ja047087Z |
0.591 |
|
| 2004 |
Liang ZX, Lee T, Resing KA, Ahn NG, Klinman JP. Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase Proceedings of the National Academy of Sciences of the United States of America. 101: 9556-9561. PMID 15210941 DOI: 10.1073/Pnas.0403337101 |
0.731 |
|
| 2004 |
Magnusson OT, Toyama H, Saeki M, Rojas A, Reed JC, Liddington RC, Klinman JP, Schwarzenbacher R. Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone Proceedings of the National Academy of Sciences of the United States of America. 101: 7913-7918. PMID 15148379 DOI: 10.1073/Pnas.0402640101 |
0.45 |
|
| 2004 |
Ceccarelli C, Liang ZX, Strickler M, Prehna G, Goldstein BM, Klinman JP, Bahnson BJ. Crystal Structure and Amide H/D Exchange of Binary Complexes of Alcohol Dehydrogenase from Bacillus stearothermophilus: Insight into Thermostability and Cofactor Binding Biochemistry. 43: 5266-5277. PMID 15122892 DOI: 10.1021/Bi049736P |
0.758 |
|
| 2004 |
Magnusson OT, Toyama H, Saeki M, Schwarzenbacher R, Klinman JP. The Structure of a Biosynthetic Intermediate of Pyrroloquinoline Quinone (PQQ) and Elucidation of the Final Step of PQQ Biosynthesis Journal of the American Chemical Society. 126: 5342-5343. PMID 15113189 DOI: 10.1021/Ja0493852 |
0.428 |
|
| 2004 |
DuBois JL, Klinman JP. Methods for characterizing TPQ-containing proteins. Methods in Enzymology. 378: 17-31. PMID 15038956 DOI: 10.1016/S0076-6879(04)78002-7 |
0.627 |
|
| 2004 |
Purdy MM, Koo LS, Ortiz de Montellano PR, Klinman JP. Steady-state kinetic investigation of cytochrome P450cam: interaction with redox partners and reaction with molecular oxygen. Biochemistry. 43: 271-81. PMID 14705955 DOI: 10.1021/Bi0356045 |
0.733 |
|
| 2003 |
Knapp MJ, Klinman JP. Kinetic studies of oxygen reactivity in soybean lipoxygenase-1. Biochemistry. 42: 11466-75. PMID 14516198 DOI: 10.1021/Bi0300884 |
0.549 |
|
| 2003 |
Evans JP, Ahn K, Klinman JP. Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase: Implications for the reactive oxygen species Journal of Biological Chemistry. 278: 49691-49698. PMID 12966104 DOI: 10.1074/Jbc.M300797200 |
0.426 |
|
| 2003 |
Mure M, Wang SX, Klinman JP. Synthesis and characterization of model compounds of the lysine tyrosyl quinone cofactor of lysyl oxidase. Journal of the American Chemical Society. 125: 6113-25. PMID 12785842 DOI: 10.1021/Ja0214274 |
0.336 |
|
| 2003 |
Tsai SC, Klinman JP. De novo design and utilization of photolabile caged substrates as probes of hydrogen tunneling with horse liver alcohol dehydrogenase at sub-zero temperatures: a cautionary note. Bioorganic Chemistry. 31: 172-90. PMID 12729574 DOI: 10.1016/S0045-2068(03)00018-X |
0.471 |
|
| 2003 |
Klinman JP. The multi-functional topa-quinone copper amine oxidases. Biochimica Et Biophysica Acta. 1647: 131-7. PMID 12686122 DOI: 10.1016/S1570-9639(03)00077-3 |
0.387 |
|
| 2003 |
Francisco WA, Blackburn NJ, Klinman JP. Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine alpha-hydroxylating monooxygenase: mechanistic implications. Biochemistry. 42: 1813-9. PMID 12590568 DOI: 10.1021/Bi020592T |
0.48 |
|
| 2003 |
Roth JP, Klinman JP. Catalysis of electron transfer during activation of O2 by the flavoprotein glucose oxidase. Proceedings of the National Academy of Sciences of the United States of America. 100: 62-7. PMID 12506204 DOI: 10.1073/Pnas.252644599 |
0.666 |
|
| 2003 |
Klinman JP. Dynamic barriers and tunneling. New views of hydrogen transfer in enzyme reactions Pure and Applied Chemistry. 75: 601-608. DOI: 10.1351/Pac200375050601 |
0.423 |
|
| 2002 |
Goto Y, Klinman JP. Binding of dioxygen to non-metal sites in proteins: exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha. Biochemistry. 41: 13637-43. PMID 12427025 DOI: 10.1021/Bi0204591 |
0.379 |
|
| 2002 |
Mills SA, Goto Y, Su Q, Plastino J, Klinman JP. Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha. Biochemistry. 41: 10577-84. PMID 12186541 DOI: 10.1021/Bi0200864 |
0.685 |
|
| 2002 |
Mure M, Mills SA, Klinman JP. Catalytic mechanism of the topa quinone containing copper amine oxidases. Biochemistry. 41: 9269-78. PMID 12135347 DOI: 10.1021/Bi020246B |
0.602 |
|
| 2002 |
Francisco WA, Knapp MJ, Blackburn NJ, Klinman JP. Hydrogen tunneling in peptidylglycine alpha-hydroxylating monooxygenase. Journal of the American Chemical Society. 124: 8194-5. PMID 12105892 DOI: 10.1021/Ja025758S |
0.577 |
|
| 2002 |
Seymour SL, Klinman JP. Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase: the relationship of modification of the protein envelope to C-H activation and tunneling. Biochemistry. 41: 8747-58. PMID 12093294 DOI: 10.1021/Bi020054G |
0.787 |
|
| 2002 |
Knapp MJ, Klinman JP. Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics. European Journal of Biochemistry / Febs. 269: 3113-21. PMID 12084051 DOI: 10.1046/J.1432-1033.2002.03022.X |
0.588 |
|
| 2002 |
Knapp MJ, Rickert K, Klinman JP. Temperature-dependent isotope effects in soybean lipoxygenase-1: correlating hydrogen tunneling with protein dynamics. Journal of the American Chemical Society. 124: 3865-74. PMID 11942823 DOI: 10.1021/Ja012205T |
0.602 |
|
| 2002 |
Green EL, Nakamura N, Dooley DM, Klinman JP, Sanders-Loehr J. Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases. Biochemistry. 41: 687-96. PMID 11781110 DOI: 10.1021/Bi011685Y |
0.383 |
|
| 2001 |
Klinman JP. How many ways to craft a cofactor? Proceedings of the National Academy of Sciences of the United States of America. 98: 14766-8. PMID 11752422 DOI: 10.1073/Pnas.011602498 |
0.386 |
|
| 2001 |
Dove JE, Klinman JP. Trihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase. Advances in Protein Chemistry. 58: 141-74. PMID 11665487 DOI: 10.1016/S0065-3233(01)58004-3 |
0.684 |
|
| 2001 |
Thrower JS, Blalock R, Klinman JP. Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase. Biochemistry. 40: 9717-24. PMID 11583172 DOI: 10.1021/Bi010329C |
0.405 |
|
| 2001 |
Knapp MJ, Seebeck FP, Klinman JP. Steric control of oxygenation regiochemistry in soybean lipoxygenase-1. Journal of the American Chemical Society. 123: 2931-2. PMID 11457000 DOI: 10.1021/Ja003855K |
0.45 |
|
| 2001 |
Tang C, Klinman JP. The catalytic function of bovine lysyl oxidase in the absence of copper. The Journal of Biological Chemistry. 276: 30575-8. PMID 11395477 DOI: 10.1074/Jbc.C100138200 |
0.389 |
|
| 2001 |
Tsai S, Klinman JP. Probes of hydrogen tunneling with horse liver alcohol dehydrogenase at subzero temperatures. Biochemistry. 40: 2303-11. PMID 11329300 DOI: 10.1021/Bi002075L |
0.417 |
|
| 2001 |
Schwartz B, Olgin AK, Klinman JP. The role of copper in topa quinone biogenesis and catalysis, as probed by azide inhibition of a copper amine oxidase from yeast. Biochemistry. 40: 2954-63. PMID 11258907 DOI: 10.1021/Bi0021378 |
0.403 |
|
| 2001 |
Klinman JP. Life as aerobes: are there simple rules for activation of dioxygen by enzymes? Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 1-13. PMID 11191216 DOI: 10.1007/S007750000172 |
0.449 |
|
| 2001 |
Schwartz B, Klinman JP. Mechanisms of biosynthesis of protein-derived redox cofactors. Vitamins and Hormones. 61: 219-39. PMID 11153267 DOI: 10.1016/S0083-6729(01)61007-0 |
0.398 |
|
| 2001 |
Stahl SS, Francisco WA, Merkx M, Klinman JP, Lippard SJ. Oxygen kinetic isotope effects in soluble methane monooxygenase. The Journal of Biological Chemistry. 276: 4549-53. PMID 11073959 DOI: 10.1074/Jbc.M008301200 |
0.306 |
|
| 2001 |
Klinman JP, Dove JE. Advances in protein chemistry: Preface Advances in Protein Chemistry. 58: ix-xi. DOI: 10.1016/S0065-3233(01)58000-6 |
0.577 |
|
| 2000 |
Chen Z, Schwartz B, Williams NK, Li R, Klinman JP, Mathews FS. Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli. Biochemistry. 39: 9709-17. PMID 10933787 DOI: 10.1021/bi000639f |
0.32 |
|
| 2000 |
Melville CR, Green EL, Sanders-Loehr J, Klinman JP. Reassessment of the active site quino-cofactor proposed to occur in the Aspergillus niger amine oxidase AO-I from the properties of model compounds. Biochemistry. 39: 7589-94. PMID 10858309 DOI: 10.1021/Bi000507M |
0.34 |
|
| 2000 |
Schwartz B, Dove JE, Klinman JP. Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast. Biochemistry. 39: 3699-707. PMID 10736169 DOI: 10.1021/Bi9922244 |
0.677 |
|
| 2000 |
Dove JE, Schwartz B, Williams NK, Klinman JP. Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast. Biochemistry. 39: 3690-8. PMID 10736168 DOI: 10.1021/Bi992225W |
0.702 |
|
| 2000 |
Chin JK, Klinman JP. Probes of a role for remote binding interactions on hydrogen tunneling in the horse liver alcohol dehydrogenase reaction. Biochemistry. 39: 1278-84. PMID 10684607 DOI: 10.1021/Bi9920331 |
0.434 |
|
| 2000 |
Kohen A, Klinman JP. Protein flexibility correlates with degree of hydrogen tunneling in thermophilic and mesophilic alcohol dehydrogenases [18] Journal of the American Chemical Society. 122: 10738-10739. DOI: 10.1021/Ja002229K |
0.691 |
|
| 2000 |
Mills SA, Klinman JP. Evidence against reduction of Cu2+ to Cu+ during dioxygen activation in a copper amine oxidase from yeast Journal of the American Chemical Society. 122: 9897-9904. DOI: 10.1021/Ja000325F |
0.641 |
|
| 2000 |
Williams NK, Klinman JP. Whence topa? Models for the biogenesis of topa quinone in copper amine oxidases Journal of Molecular Catalysis - B Enzymatic. 8: 95-101. DOI: 10.1016/S1381-1177(99)00071-5 |
0.371 |
|
| 1999 |
Rickert KW, Klinman JP. Nature of hydrogen transfer in soybean lipoxygenase 1: separation of primary and secondary isotope effects. Biochemistry. 38: 12218-28. PMID 10493789 DOI: 10.1021/Bi990834Y |
0.416 |
|
| 1999 |
Stewart L, Klinman JP. Kinetic parameters for dimeric and tetrameric forms of bovine dopamine beta-monooxygenase and their relationship to non-Michaelis-Menten behavior. Febs Letters. 454: 229-32. PMID 10431813 DOI: 10.1016/S0014-5793(99)00761-9 |
0.385 |
|
| 1999 |
Su Q, Klinman JP. Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation. Biochemistry. 38: 8572-81. PMID 10387105 DOI: 10.1021/Bi990044O |
0.378 |
|
| 1999 |
Plastino J, Green EL, Sanders-Loehr J, Klinman JP. An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha. Biochemistry. 38: 8204-16. PMID 10387066 DOI: 10.1021/Bi9826660 |
0.466 |
|
| 1999 |
Kohen A, Klinman JP. Hydrogen tunneling in biology. Chemistry & Biology. 6: R191-8. PMID 10381408 DOI: 10.1016/S1074-5521(99)80058-1 |
0.671 |
|
| 1999 |
Kohen A, Cannio R, Bartolucci S, Klinman JP. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase. Nature. 399: 496-9. PMID 10365965 DOI: 10.1038/20981 |
0.748 |
|
| 1999 |
Hevel JM, Mills SA, Klinman JP. Mutation of a strictly conserved, active-site residue alters substrate specificity and cofactor biogenesis in a copper amine oxidase. Biochemistry. 38: 3683-93. PMID 10090756 DOI: 10.1021/Bi982199M |
0.68 |
|
| 1999 |
Rucker J, Klinman JP. Computational study of tunneling and coupled motion in alcohol dehydrogenase-catalyzed reactions: Implication for measured hydrogen and carbon isotope effects Journal of the American Chemical Society. 121: X. DOI: 10.1021/Ja9824425 |
0.386 |
|
| 1998 |
Schwartz B, Green EL, Sanders-Loehr J, Klinman JP. Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast. Biochemistry. 37: 16591-600. PMID 9843426 DOI: 10.1021/Bi981541S |
0.444 |
|
| 1998 |
Su Q, Klinman JP. Probing the mechanism of proton coupled electron transfer to dioxygen: the oxidative half-reaction of bovine serum amine oxidase. Biochemistry. 37: 12513-25. PMID 9730824 DOI: 10.1021/Bi981103L |
0.464 |
|
| 1998 |
Colby TD, Bahnson BJ, Chin JK, Klinman JP, Goldstein BM. Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes. Biochemistry. 37: 9295-304. PMID 9649310 DOI: 10.1021/Bi973184B |
0.736 |
|
| 1998 |
Francisco WA, Merkler DJ, Blackburn NJ, Klinman JP. Kinetic mechanism and intrinsic isotope effects for the peptidylglycine alpha-amidating enzyme reaction. Biochemistry. 37: 8244-52. PMID 9609721 DOI: 10.1021/Bi973004Y |
0.412 |
|
| 1998 |
Li R, Klinman JP, Mathews FS. Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4 A resolution reveals the active conformation. Structure (London, England : 1993). 6: 293-307. PMID 9551552 DOI: 10.1016/S0969-2126(98)00033-1 |
0.465 |
|
| 1998 |
Francisco WA, Tian G, Fitzpatrick PF, Klinman JP. Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: Evidence of rate limiting oxygen activation Journal of the American Chemical Society. 120: 4057-4062. DOI: 10.1021/Ja973543Q |
0.397 |
|
| 1998 |
Kohen A, Klinman JP. Enzyme Catalysis: Beyond Classical Paradigms Accounts of Chemical Research. 31: 397-404. DOI: 10.1021/Ar9701225 |
0.756 |
|
| 1997 |
Bahnson BJ, Colby TD, Chin JK, Goldstein BM, Klinman JP. A link between protein structure and enzyme catalyzed hydrogen tunneling. Proceedings of the National Academy of Sciences of the United States of America. 94: 12797-802. PMID 9371755 DOI: 10.1073/Pnas.94.24.12797 |
0.746 |
|
| 1997 |
Wang SX, Nakamura N, Mure M, Klinman JP, Sanders-Loehr J. Characterization of the native lysine tyrosylquinone cofactor in lysyl oxidase by Raman spectroscopy. The Journal of Biological Chemistry. 272: 28841-4. PMID 9360949 DOI: 10.1074/Jbc.272.46.28841 |
0.398 |
|
| 1997 |
Cai D, Dove J, Nakamura N, Sanders-Loehr J, Klinman JP. Mechanism-based inactivation of a yeast methylamine oxidase mutant: implications for the functional role of the consensus sequence surrounding topaquinone. Biochemistry. 36: 11472-8. PMID 9298967 DOI: 10.1021/Bi970812G |
0.731 |
|
| 1997 |
Cai D, Williams NK, Klinman JP. Effect of metal on 2,4,5-trihydroxyphenylalanine (topa) quinone biogenesis in the Hansenula polymorpha copper amine oxidase. The Journal of Biological Chemistry. 272: 19277-81. PMID 9235922 DOI: 10.1074/Jbc.272.31.19277 |
0.367 |
|
| 1997 |
Kohen A, Jonsson T, Klinman JP. Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction. Biochemistry. 36: 2603-11. PMID 9054567 DOI: 10.1021/Bi962492R |
0.744 |
|
| 1997 |
Glickman MH, Cliff S, Thiemens M, Klinman JP. Comparative study of 17O and 18O isotope effects as a probe for dioxygen activation: Application to the soybean lipoxygenase reaction Journal of the American Chemical Society. 119: 11357. DOI: 10.1021/Ja970689G |
0.309 |
|
| 1997 |
Wang SX, Klinman JP, Medzihradszky KF, Burlingame AL. The isolation and characterization of active site peptides in lysyl oxidase Techniques in Protein Chemistry. 8: 351-361. DOI: 10.1016/S1080-8914(97)80036-1 |
0.389 |
|
| 1997 |
Kohen A, Jonsson T, Klinman JP. Effects of enzyme glycosylation on the chemical step of catalysis, as probed by hydrogen tunneling and enthalpy of activation Techniques in Protein Chemistry. 8: 311-319. DOI: 10.1016/S1080-8914(97)80032-4 |
0.757 |
|
| 1997 |
Hevel JM, Mills SA, Klinman JP. A key residue in yeast copper amine oxidase functions in both amine oxidase activity and topa quinone biogenesis Faseb Journal. 11: A1320. |
0.571 |
|
| 1996 |
Klinman JP. Mechanisms Whereby Mononuclear Copper Proteins Functionalize Organic Substrates. Chemical Reviews. 96: 2541-2562. PMID 11848836 DOI: 10.1021/Cr950047G |
0.377 |
|
| 1996 |
Dove JE, Smith AJ, Kuchar J, Brown DE, Dooley DM, Klinman JP. Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris. Febs Letters. 398: 231-4. PMID 8977113 DOI: 10.1016/S0014-5793(96)01245-8 |
0.665 |
|
| 1996 |
Glickman MH, Klinman JP. Lipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover. Biochemistry. 35: 12882-92. PMID 8841132 DOI: 10.1021/Bi960985Q |
0.413 |
|
| 1996 |
Wang SX, Mure M, Medzihradszky KF, Burlingame AL, Brown DE, Dooley DM, Smith AJ, Kagan HM, Klinman JP. A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. Science (New York, N.Y.). 273: 1078-84. PMID 8688089 DOI: 10.1126/Science.273.5278.1078 |
0.348 |
|
| 1996 |
Colby TD, Bahnson BJ, Chin JK, Klinman JP, Goldstein BM. Two mutations in the active site of alcohol dehydrogenase perturb the catalytic geometry Acta Crystallographica Section a Foundations of Crystallography. 52: C101-C101. DOI: 10.1107/S0108767396095098 |
0.652 |
|
| 1996 |
Jonsson T, Glickman MH, Sun S, Klinman JP. Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis Journal of the American Chemical Society. 118: 10319-10320. DOI: 10.1021/Ja961827P |
0.425 |
|
| 1995 |
Mu D, Klinman JP. Cloning of mammalian topa quinone-containing enzymes. Methods in Enzymology. 258: 114-22. PMID 8524143 DOI: 10.1016/0076-6879(95)58040-9 |
0.367 |
|
| 1995 |
Bahnson BJ, Klinman JP. Hydrogen tunneling in enzyme catalysis. Methods in Enzymology. 249: 373-97. PMID 7791619 DOI: 10.1016/0076-6879(95)49042-6 |
0.733 |
|
| 1995 |
Moënne-Loccoz P, Nakamura N, Steinebach V, Duine JA, Mure M, Klinman JP, Sanders-Loehr J. Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy. Biochemistry. 34: 7020-6. PMID 7766611 DOI: 10.1021/Bi00021A013 |
0.357 |
|
| 1995 |
Glickman MH, Klinman JP. Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction. Biochemistry. 34: 14077-92. PMID 7578005 DOI: 10.1021/Bi00043A013 |
0.451 |
|
| 1995 |
Plastino J, Klinman JP. Limited proteolysis of Hansenula polymorpha yeast amine oxidase: isolation of a C-terminal fragment containing both a copper and quino-cofactor. Febs Letters. 371: 276-8. PMID 7556609 DOI: 10.1016/0014-5793(95)00907-Q |
0.323 |
|
| 1995 |
Mure M, Klinman JP. Model studies of topaquinone-dependent amine oxidases. 2. Characterization of reaction intermediates and mechanism Journal of the American Chemical Society. 117: 8707-8718. DOI: 10.1021/Ja00139A003 |
0.323 |
|
| 1994 |
Tian G, Berry JA, Klinman JP. Oxygen-18 kinetic isotope effects in the dopamine beta-monooxygenase reaction: evidence for a new chemical mechanism in non-heme metallomonooxygenases. Biochemistry. 33: 226-34. PMID 8286345 DOI: 10.1021/Bi00167A030 |
0.405 |
|
| 1994 |
Cai D, Klinman JP. Copper amine oxidase: heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae. Biochemistry. 33: 7647-53. PMID 8011631 DOI: 10.1021/Bi00190A019 |
0.448 |
|
| 1994 |
Jonsson T, Edmondson DE, Klinman JP. Hydrogen tunneling in the flavoenzyme monoamine oxidase B. Biochemistry. 33: 14871-8. PMID 7993913 DOI: 10.1021/Bi00253A026 |
0.373 |
|
| 1994 |
Cai D, Klinman JP. Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. The Journal of Biological Chemistry. 269: 32039-42. PMID 7798196 |
0.309 |
|
| 1993 |
Bahnson BJ, Park DH, Kim K, Plapp BV, Klinman JP. Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis. Biochemistry. 32: 5503-7. PMID 8504071 DOI: 10.1021/Bi00072A003 |
0.726 |
|
| 1993 |
Klinman JP. Spectroscopic detection of chemical intermediates in the reaction of para-substituted benzylamines with bovine serum amine oxidase Biochemistry. 32: 2234-2241. PMID 8443165 DOI: 10.1021/Bi00060A015 |
0.373 |
|
| 1993 |
Tian G, Klinman JP. Discrimination between 16O and 18O in oxygen binding to the reversible oxygen carriers hemoglobin, myoglobin, hemerythrin, and hemocyanin: A new probe for oxygen binding and reductive activation by proteins Journal of the American Chemical Society. 115: X-8897. DOI: 10.1021/Ja00073A001 |
0.328 |
|
| 1993 |
Mure M, Klinman JP. Synthesis and spectroscopic characterization of model compounds for the active site cofactor in copper amine oxidases Journal of the American Chemical Society. 115: 7117-7127. DOI: 10.1021/Ja00069A008 |
0.321 |
|
| 1992 |
Rucker J, Cha Y, Jonsson T, Grant KL, Klinman JP. Role of internal thermodynamics in determining hydrogen tunneling in enzyme-catalyzed hydrogen transfer reactions Biochemistry. 31: 11489-11499. PMID 1445883 DOI: 10.1021/Bi00161A030 |
0.442 |
|
| 1992 |
Janes SM, Palcic MM, Scaman CH, Smith AJ, Brown DE, Dooley DM, Mure M, Klinman JP. Identification of topaquinone and its consensus sequence in copper amine oxidases Biochemistry. 31: 12147-12154. DOI: 10.1021/Bi00163A025 |
0.384 |
|
| 1992 |
Grant KL, Klinman JP. Exponential relationships among multiple hydrogen isotope effects as probes of hydrogen tunneling Bioorganic Chemistry. 20: 1-7. DOI: 10.1016/0045-2068(92)90021-T |
0.328 |
|
| 1992 |
Klinman JP, Berry JA, Tian G. New Probes of Oxygen Binding and Activation: Application to Dopamine β-Monooxygenase Journal of Inorganic Biochemistry. 47: 151-163. DOI: 10.1007/978-94-011-6875-5_13 |
0.419 |
|
| 1991 |
Janes SM, Klinman JP. An investigation of bovine serum amine oxidase active site stoichiometry: evidence for an aminotransferase mechanism involving two carbonyl cofactors per enzyme dimer Biochemistry. 30: 4599-4605. PMID 2021652 DOI: 10.1021/Bi00232A034 |
0.46 |
|
| 1991 |
Kim SC, Klinman JP. Mechanism of inhibition of dopamine β-monooxygenase by quinol and phenol derivatives, as determined by solvent and substrate deuterium isotope effects Biochemistry. 30: 8138-8144. PMID 1868089 DOI: 10.1021/Bi00247A007 |
0.354 |
|
| 1991 |
Klinman JP, Dooley DM, Duine JA, Knowles PF, Mondovi B, Villafranca JJ. Status of the cofactor identity in copper oxidative enzymes. Febs Letters. 282: 1-4. PMID 1851106 DOI: 10.1016/0014-5793(91)80431-2 |
0.408 |
|
| 1991 |
Klinman JP. Surprises among quinoproteins Current Opinion in Structural Biology. 1: 968-972. DOI: 10.1016/0959-440X(91)90092-8 |
0.418 |
|
| 1990 |
Klinman JP. Quantum mechanical effects in enzyme-catalysed hydrogen transfer reactions. Trends in Biochemical Sciences. 14: 368-73. PMID 2688201 DOI: 10.1016/0968-0004(89)90010-8 |
0.444 |
|
| 1990 |
Hartmann C, Klinman JP. Reductive trapping of substrate to methylamine oxidase from Arthrobacter P1 Febs Letters. 261: 441-444. PMID 2155832 DOI: 10.1016/0014-5793(90)80611-L |
0.436 |
|
| 1990 |
Janes SM, Mu D, Wemmer D, Smith AJ, Kaur S, Maltby D, Burlingame AL, Klinman JP. A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science (New York, N.Y.). 248: 981-7. PMID 2111581 DOI: 10.1126/Science.2111581 |
0.409 |
|
| 1989 |
Klinman JP, Janes S, Hartmann C. Mechanism of reaction of the copper amine oxidases. Pharmacological Research Communications. 35-7. PMID 2854269 DOI: 10.1016/S0031-6989(88)80544-7 |
0.303 |
|
| 1989 |
Grant KL, Klinman JP. Evidence that both protium and deuterium undergo significant tunneling in the reaction catalyzed by bovine serum amine oxidase Biochemistry. 28: 6597-6605. PMID 2790014 DOI: 10.1021/Bi00442A010 |
0.369 |
|
| 1989 |
Cha Y, Murray CJ, Klinman JP. Hydrogen tunneling in enzyme reactions Science. 243: 1325-1330. PMID 2646716 DOI: 10.1126/Science.2646716 |
0.352 |
|
| 1989 |
Brenner MC, Klinman JP. Correlation of copper valency with product formation in single turnovers of dopamine beta-monooxygenase. Biochemistry. 28: 4664-70. PMID 2548587 DOI: 10.1021/Bi00437A023 |
0.39 |
|
| 1989 |
Brenner MC, Murray CJ, Klinman JP. Rapid freeze- and chemical-quench studies of dopamine beta-monooxygenase: comparison of pre-steady-state and steady-state parameters. Biochemistry. 28: 4656-64. PMID 2548586 DOI: 10.1021/Bi00437A022 |
0.364 |
|
| 1987 |
Farnum MF, Klinman JP. Stereochemical probes of bovine plasma amine oxidase: evidence for mirror image processing and a syn abstraction of hydrogens from C-1 and C-2 of dopamine. Biochemistry. 25: 6028-36. PMID 3790504 DOI: 10.1021/Bi00368A029 |
0.336 |
|
| 1987 |
Stewart LC, Klinman JP. Characterization of alternate reductant binding and electron transfer in the dopamine beta-monooxygenase reaction. Biochemistry. 26: 5302-9. PMID 3676254 DOI: 10.1021/Bi00391A013 |
0.388 |
|
| 1986 |
Farnum M, Palcic M, Klinman JP. pH dependence of deuterium isotope effects and tritium exchange in the bovine plasma amine oxidase reaction: a role for single-base catalysis in amine oxidation and imine exchange. Biochemistry. 25: 1898-904. PMID 3518796 DOI: 10.1021/Bi00356A010 |
0.414 |
|
| 1985 |
Miller SM, Klinman JP. Secondary isotope effects and structure-reactivity correlations in the dopamine beta-monooxygenase reaction: evidence for a chemical mechanism. Biochemistry. 24: 2114-27. PMID 3995006 DOI: 10.1021/Bi00330A004 |
0.429 |
|
| 1985 |
Klinman JP, Matthews RG. Calculation of substrate dissociation constants from steady-state isotope effects in enzyme-catalyzed reactions Journal of the American Chemical Society. 107: 1058-1060. DOI: 10.1002/Chin.198527085 |
0.391 |
|
| 1984 |
Palcic MM, Klinman JP. Isotopic probes yield microscopic constants: separation of binding energy from catalytic efficiency in the bovine plasma amine oxidase reaction. Biochemistry. 22: 5957-66. PMID 6661419 DOI: 10.1021/Bi00294A040 |
0.433 |
|
| 1983 |
Miller SM, Klinman JP. Deduction of kinetic mechanisms from primary hydrogen isotope effects: dopamine beta-monooxygenase--a case history. Methods in Enzymology. 87: 711-32. PMID 7176929 DOI: 10.1016/S0076-6879(82)87036-5 |
0.426 |
|
| 1983 |
Ahn N, Klinman JP. Mechanism of modulation of dopamine β-monooxygenase by pH and fumarate as deduced from initial rate and primary deuterium isotope effect studies Biochemistry. 22: 3096-3106. PMID 6882739 DOI: 10.1021/Bi00282A012 |
0.625 |
|
| 1983 |
Miller SM, Klinman JP. Magnitude of intrinsic isotope effects in the dopamine beta-monooxygenase reaction. Biochemistry. 22: 3091-6. PMID 6882738 DOI: 10.1021/Bi00282A011 |
0.434 |
|
| 1981 |
Klinman JP. Probes of mechanism and transition-state structure in the alcohol dehydrogenase reaction. Crc Critical Reviews in Biochemistry. 10: 39-78. PMID 7011676 DOI: 10.3109/10409238109114635 |
0.316 |
|
| 1980 |
Welsh KM, Creighton DJ, Klinman JP. Transition-state structure in the yeast alcohol dehydrogenase reaction: the magnitude of solvent and alpha-secondary hydrogen isotope effects. Biochemistry. 19: 2005-16. PMID 6990968 DOI: 10.1021/Bi00551A001 |
0.388 |
|
| 1979 |
Battersby AR, Staunton J, Klinman J, Summers MC. Stereochemistry of oxidation of benzylamine by the amine oxidase from beef plasma. Febs Letters. 99: 297-8. PMID 428554 DOI: 10.1016/0014-5793(79)80976-X |
0.386 |
|
| 1978 |
Klinman JP. Kinetic isotope effects in enzymology. Advances in Enzymology and Related Areas of Molecular Biology. 46: 415-94. PMID 345770 DOI: 10.1002/9780470122914.Ch7 |
0.317 |
|
| 1976 |
Klinman JP, Welsh K. The zinc content of yeast alcohol dehydrogenase. Biochemical and Biophysical Research Communications. 70: 878-84. PMID 779786 DOI: 10.1016/0006-291X(76)90673-2 |
0.385 |
|
| 1976 |
Klinman JP. Isotope effects and structure-reactivity correlations in the yeast alcohol dehydrogenase reaction. A study of the enzyme-catalyzed oxidation of aromatic alcohols. Biochemistry. 15: 2018-26. PMID 773429 DOI: 10.1021/Bi00654A032 |
0.35 |
|
| 1975 |
Klinman JP. The interaction of an epoxide with yeast alcohol dehydrogenase: evidence for binding and the modification of two active site cysteines by styrene oxide. Biochemistry. 14: 2568-74. PMID 238561 DOI: 10.1021/Bi00683A002 |
0.403 |
|
| 1974 |
Schray K, Klinman JP. The magnitude of enzyme transition state analog binding constants. Biochemical and Biophysical Research Communications. 57: 641-8. PMID 4827826 DOI: 10.1016/0006-291X(74)90594-4 |
0.406 |
|
| 1971 |
Klinman JP, Rose IA. Stereochemistry of the interconversions of citrate and acetate catalyzed by citrate synthase, adenosine triphosphate citrate lyase, and citrate lyase. Biochemistry. 10: 2267-72. PMID 5165527 DOI: 10.1021/Bi00788A013 |
0.577 |
|
| 1971 |
Klinman JP, Rose IA. Mechanism of the aconitate isomerase reaction. Biochemistry. 10: 2259-66. PMID 5114988 DOI: 10.1021/Bi00788A012 |
0.552 |
|
| 1971 |
Klinman JP, Rose IA. Purification and kinetic properties of aconitate isomerase from Pseudomonas putida. Biochemistry. 10: 2253-9. PMID 5114987 DOI: 10.1021/Bi00788A011 |
0.559 |
|
| 1971 |
Klinman JP, Samuel D. Oxygen-18 studies to determine the position of bond cleavage of acetyl phosphate in the presence of divalent metal ions. Biochemistry. 10: 2126-31. PMID 4327401 DOI: 10.1021/Bi00787A026 |
0.531 |
|
| 1968 |
Klinman JP, Thornton ER. Solvolysis mechanisms. A kinetic study of the hydrolysis and imidazole-catalyzed hydrolysis of p-methyl-, p-chloro-, and p-nitrobenzoylimidazole in H2O and of p-nitrobenzoylimidazole in deuterium oxide Journal of the American Chemical Society. 90: 4390-4394. DOI: 10.1021/Ja01018A034 |
0.584 |
|
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