| Year |
Citation |
Score |
| 2023 |
Babicz JT, Rogers MS, DeWeese DE, Sutherlin KD, Banerjee R, Böttger LH, Yoda Y, Nagasawa N, Saito M, Kitao S, Kurokuzu M, Kobayashi Y, Tamasaku K, Seto M, Lipscomb JD, et al. Nuclear Resonance Vibrational Spectroscopy Definition of Peroxy Intermediates in Catechol Dioxygenases: Factors that Determine Extra- versus Intradiol Cleavage. Journal of the American Chemical Society. PMID 37414058 DOI: 10.1021/jacs.3c02242 |
0.589 |
|
| 2022 |
Rogers MS, Gordon AM, Rappe TM, Goodpaster JD, Lipscomb JD. Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase. Biochemistry. 62: 507-523. PMID 36583545 DOI: 10.1021/acs.biochem.2c00610 |
0.402 |
|
| 2022 |
Cutsail GE, Banerjee R, Rice DB, McCubbin Stepanic O, Lipscomb JD, DeBeer S. Determination of the iron(IV) local spin states of the Q intermediate of soluble methane monooxygenase by Kβ X-ray emission spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 35988092 DOI: 10.1007/s00775-022-01953-4 |
0.538 |
|
| 2021 |
Jones JC, Banerjee R, Semonis MM, Shi K, Aihara H, Lipscomb JD. X-ray Crystal Structures of Methane Monooxygenase Hydroxylase Complexes with Variants of Its Regulatory Component: Correlations with Altered Reaction Cycle Dynamics. Biochemistry. PMID 34910460 DOI: 10.1021/acs.biochem.1c00673 |
0.519 |
|
| 2021 |
Jacobs AB, Banerjee R, Deweese DE, Braun A, Babicz JT, Gee LB, Sutherlin KD, Böttger LH, Yoda Y, Saito M, Kitao S, Kobayashi Y, Seto M, Tamasaku K, Lipscomb JD, et al. Nuclear Resonance Vibrational Spectroscopic Definition of the Fe(IV) Intermediate Q in Methane Monooxygenase and Its Reactivity. Journal of the American Chemical Society. PMID 34570980 DOI: 10.1021/jacs.1c05436 |
0.507 |
|
| 2021 |
Jones JC, Banerjee R, Shi K, Semonis MM, Aihara H, Pomerantz WCK, Lipscomb JD. Soluble Methane Monooxygenase Component Interactions Monitored by F NMR. Biochemistry. PMID 34100595 DOI: 10.1021/acs.biochem.1c00293 |
0.51 |
|
| 2021 |
Banerjee R, Lipscomb JD. Small-Molecule Tunnels in Metalloenzymes Viewed as Extensions of the Active Site. Accounts of Chemical Research. PMID 33886257 DOI: 10.1021/acs.accounts.1c00058 |
0.504 |
|
| 2020 |
Jones JC, Banerjee R, Shi K, Aihara H, Lipscomb JD. Structural Studies of OB3b Soluble Methane Monooxygenase Hydroxylase and Regulatory Component Complex Reveal a Transient Substrate Tunnel. Biochemistry. PMID 32692178 DOI: 10.1021/Acs.Biochem.0C00459 |
0.579 |
|
| 2020 |
Srinivas V, Banerjee R, Lebrette H, Jones JC, Aurelius O, Kim IS, Pham CC, Gul S, Sutherlin K, Bhowmick A, John J, Bozkurt E, Fransson T, Aller P, Butryn A, ... ... Lipscomb JD, et al. High Resolution XFEL Structure of the Soluble Methane Monooxygenase Hydroxylase Complex with its Regulatory Component at Ambient Temperature in Two Oxidation States. Journal of the American Chemical Society. PMID 32683863 DOI: 10.1021/Jacs.0C05613 |
0.568 |
|
| 2019 |
Rogers MS, Lipscomb JD. Salicylate 5-Hydroxylase: Intermediates in Aromatic Hydroxylation by a Rieske Monooxygenase. Biochemistry. PMID 31066545 DOI: 10.1021/Acs.Biochem.9B00292 |
0.533 |
|
| 2019 |
Banerjee R, Jones JC, Lipscomb JD. Soluble Methane Monooxygenase. Annual Review of Biochemistry. PMID 30633550 DOI: 10.1146/Annurev-Biochem-013118-111529 |
0.576 |
|
| 2018 |
Sutherlin KD, Wasada-Tsutsui Y, Mbughuni MM, Rogers MS, Park K, Liu LV, Kwak Y, Srnec M, Böttger LH, Frenette M, Yoda Y, Kobayashi Y, Kurokuzu M, Saito M, Seto M, ... ... Lipscomb JD, et al. NRVS definition of O intermediates in an extradiol dioxygenase: correlation to crystallography and reactivity. Journal of the American Chemical Society. PMID 30418018 DOI: 10.1021/Jacs.8B06517 |
0.826 |
|
| 2018 |
Cutsail Iii GE, Banerjee R, Zhou A, Que L, Lipscomb JD, DeBeer S. High-Resolution EXAFS Provides Evidence for a Longer Fe•••Fe Distance in the Q Intermediate of Methane Monooxygenase. Journal of the American Chemical Society. PMID 30398343 DOI: 10.1021/Jacs.8B10313 |
0.662 |
|
| 2018 |
Sutherlin KD, Rivard BS, Böttger LH, Liu LV, Rogers MS, Srnec M, Park K, Yoda Y, Kitao S, Kobayashi Y, Saito M, Seto M, Hu M, Zhao J, Lipscomb JD, et al. NRVS studies of the peroxide shunt intermediate in a Rieske dioxygenase and its relation to the native FeOreaction. Journal of the American Chemical Society. PMID 29618204 DOI: 10.1021/Jacs.8B01822 |
0.464 |
|
| 2018 |
Komor AJ, Jasniewski AJ, Que L, Lipscomb JD. Diiron monooxygenases in natural product biosynthesis. Natural Product Reports. PMID 29552683 DOI: 10.1039/C7Np00061H |
0.639 |
|
| 2017 |
Castillo RG, Banerjee R, Allpress CJ, Rohde GT, Bill E, Que L, Lipscomb JD, DeBeer S. High-Energy Resolution Fluorescence Detected X-ray Absorption of the Q intermediate of Soluble Methane Monooxygenase. Journal of the American Chemical Society. PMID 29136468 DOI: 10.1021/Jacs.7B09560 |
0.675 |
|
| 2017 |
Oloo WN, Banerjee R, Lipscomb JD, Que L. Equilibrating (L)Fe(III)-OOAc and (L)Fe(V)(O) Species in Hydrocarbon Oxidations by Bio-Inspired Nonheme Iron Catalysts using H2O2 and AcOH. Journal of the American Chemical Society. PMID 29136467 DOI: 10.1021/Jacs.7B06246 |
0.706 |
|
| 2017 |
Banerjee R, Komor AJ, Lipscomb JD. Use of Isotopes and Isotope Effects for Investigations of Diiron Oxygenase Mechanisms. Methods in Enzymology. 596: 239-290. PMID 28911774 DOI: 10.1016/Bs.Mie.2017.07.016 |
0.52 |
|
| 2017 |
Komor AJ, Rivard BS, Fan R, Guo Y, Que L, Lipscomb JD. CmlI N-Oxygenase Catalyzes the Final Three Steps in Chloramphenicol Biosynthesis without Dissociation of Intermediates. Biochemistry. PMID 28823151 DOI: 10.1021/Acs.Biochem.7B00695 |
0.668 |
|
| 2017 |
Jasniewski AJ, Komor AJ, Lipscomb JD, Que L. An Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI. Journal of the American Chemical Society. PMID 28673082 DOI: 10.1021/Jacs.7B05389 |
0.677 |
|
| 2016 |
Jasniewski AJ, Knoot CJ, Lipscomb JD, Que L. A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase. Biochemistry. PMID 27668828 DOI: 10.1021/Acs.Biochem.6B00834 |
0.617 |
|
| 2016 |
Meier KK, Rogers MS, Kovaleva EG, Lipscomb JD, Bominaar EL, Münck E. Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies. Inorganic Chemistry. PMID 27275865 DOI: 10.1021/Acs.Inorgchem.6B00148 |
0.475 |
|
| 2016 |
Knoot CJ, Kovaleva EG, Lipscomb JD. Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27229511 DOI: 10.1007/S00775-016-1363-X |
0.447 |
|
| 2016 |
Komor AJ, Rivard BS, Fan R, Guo Y, Que L, Lipscomb JD. Mechanism for Six-Electron Aryl-N-oxygenation by the Non-Heme Diiron Enzyme CmlI. Journal of the American Chemical Society. PMID 27203126 DOI: 10.1021/Jacs.6B03341 |
0.637 |
|
| 2015 |
Meier KK, Rogers MS, Kovaleva EG, Mbughuni MM, Bominaar EL, Lipscomb JD, Münck E. A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mössbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods. Inorganic Chemistry. 54: 10269-80. PMID 26485328 DOI: 10.1021/Acs.Inorgchem.5B01576 |
0.838 |
|
| 2015 |
Kovaleva EG, Rogers MS, Lipscomb JD. Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200. Biochemistry. 54: 5329-39. PMID 26267790 DOI: 10.1021/Acs.Biochem.5B00709 |
0.438 |
|
| 2015 |
Rivard BS, Rogers MS, Marell DJ, Neibergall MB, Chakrabarty S, Cramer CJ, Lipscomb JD. Rate-Determining Attack on Substrate Precedes Rieske Cluster Oxidation during Cis-Dihydroxylation by Benzoate Dioxygenase. Biochemistry. 54: 4652-64. PMID 26154836 DOI: 10.1021/Acs.Biochem.5B00573 |
0.837 |
|
| 2015 |
Banerjee R, Proshlyakov Y, Lipscomb JD, Proshlyakov DA. Structure of the key species in the enzymatic oxidation of methane to methanol. Nature. 518: 431-4. PMID 25607364 DOI: 10.1038/Nature14160 |
0.569 |
|
| 2015 |
Makris TM, Vu VV, Meier KK, Komor AJ, Rivard BS, Münck E, Que L, Lipscomb JD. An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway. Journal of the American Chemical Society. 137: 1608-17. PMID 25564306 DOI: 10.1021/Ja511649N |
0.648 |
|
| 2015 |
Knoot CJ, Purpero VM, Lipscomb JD. Crystal structures of alkylperoxo and anhydride intermediates in an intradiol ring-cleaving dioxygenase. Proceedings of the National Academy of Sciences of the United States of America. 112: 388-93. PMID 25548185 DOI: 10.1073/Pnas.1419118112 |
0.5 |
|
| 2014 |
Su S, Panmanee W, Wilson JJ, Mahtani HK, Li Q, Vanderwielen BD, Makris TM, Rogers M, McDaniel C, Lipscomb JD, Irvin RT, Schurr MJ, Lancaster JR, Kovall RA, Hassett DJ. Catalase (KatA) plays a role in protection against anaerobic nitric oxide in Pseudomonas aeruginosa. Plos One. 9: e91813. PMID 24663218 DOI: 10.1371/Journal.Pone.0091813 |
0.37 |
|
| 2014 |
Fielding AJ, Lipscomb JD, Que L. A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 19: 491-504. PMID 24615282 DOI: 10.1007/S00775-014-1122-9 |
0.806 |
|
| 2013 |
Aukema KG, Makris TM, Stoian SA, Richman JE, Münck E, Lipscomb JD, Wackett LP. Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes. Acs Catalysis. 3: 2228-2238. PMID 24490119 DOI: 10.1021/Cs400484M |
0.425 |
|
| 2013 |
Makris TM, Knoot CJ, Wilmot CM, Lipscomb JD. Structure of a dinuclear iron cluster-containing β-hydroxylase active in antibiotic biosynthesis. Biochemistry. 52: 6662-71. PMID 23980641 DOI: 10.1021/Bi400845B |
0.415 |
|
| 2013 |
Hayden JA, Farquhar ER, Que L, Lipscomb JD, Hendrich MP. NO binding to Mn-substituted homoprotocatechuate 2,3-dioxygenase: relationship to O₂ reactivity. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 18: 717-28. PMID 23824380 DOI: 10.1007/S00775-013-1016-2 |
0.661 |
|
| 2013 |
Banerjee R, Meier KK, Münck E, Lipscomb JD. Intermediate P* from soluble methane monooxygenase contains a diferrous cluster. Biochemistry. 52: 4331-42. PMID 23718184 DOI: 10.1021/Bi400182Y |
0.621 |
|
| 2012 |
Kovaleva EG, Lipscomb JD. Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation. Biochemistry. 51: 8755-63. PMID 23066739 DOI: 10.1021/Bi301115C |
0.494 |
|
| 2012 |
Mbughuni MM, Meier KK, Münck E, Lipscomb JD. Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant. Biochemistry. 51: 8743-54. PMID 23066705 DOI: 10.1021/Bi301114X |
0.839 |
|
| 2012 |
Thompson JW, Salahudeen AA, Chollangi S, Ruiz JC, Brautigam CA, Makris TM, Lipscomb JD, Tomchick DR, Bruick RK. Structural and molecular characterization of iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5). The Journal of Biological Chemistry. 287: 7357-65. PMID 22253436 DOI: 10.1074/Jbc.M111.308684 |
0.349 |
|
| 2012 |
Fielding AJ, Lipscomb JD, Que L. Characterization of an O2 adduct of an active cobalt-substituted extradiol-cleaving catechol dioxygenase. Journal of the American Chemical Society. 134: 796-9. PMID 22175783 DOI: 10.1021/Ja2095365 |
0.802 |
|
| 2011 |
Mbughuni MM, Chakrabarti M, Hayden JA, Meier KK, Dalluge JJ, Hendrich MP, Münck E, Lipscomb JD. Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates. Biochemistry. 50: 10262-74. PMID 22011290 DOI: 10.1021/Bi201436N |
0.837 |
|
| 2011 |
Vu VV, Makris TM, Lipscomb JD, Que L. Active-site structure of a β-hydroxylase in antibiotic biosynthesis. Journal of the American Chemical Society. 133: 6938-41. PMID 21506543 DOI: 10.1021/Ja201822V |
0.622 |
|
| 2011 |
Fielding AJ, Kovaleva EG, Farquhar ER, Lipscomb JD, Que L. A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 16: 341-55. PMID 21153851 DOI: 10.1007/S00775-010-0732-0 |
0.811 |
|
| 2010 |
Mbughuni MM, Chakrabarti M, Hayden JA, Bominaar EL, Hendrich MP, Münck E, Lipscomb JD. Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Proceedings of the National Academy of Sciences of the United States of America. 107: 16788-93. PMID 20837547 DOI: 10.1073/Pnas.1010015107 |
0.827 |
|
| 2010 |
Makris TM, Chakrabarti M, Münck E, Lipscomb JD. A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 107: 15391-6. PMID 20713732 DOI: 10.1073/Pnas.1007953107 |
0.39 |
|
| 2009 |
Lipscomb JD. Oxygen Activation by Non-Heme Iron Enzymes: A Ring-Side Seat. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 5-7. PMID 21151807 DOI: 10.1007/S00775-009-0523-7 |
0.516 |
|
| 2008 |
Lipscomb JD. Mechanism of extradiol aromatic ring-cleaving dioxygenases. Current Opinion in Structural Biology. 18: 644-9. PMID 19007887 DOI: 10.1016/J.Sbi.2008.11.001 |
0.489 |
|
| 2008 |
Gunderson WA, Zatsman AI, Emerson JP, Farquhar ER, Que L, Lipscomb JD, Hendrich MP. Electron paramagnetic resonance detection of intermediates in the enzymatic cycle of an extradiol dioxygenase. Journal of the American Chemical Society. 130: 14465-7. PMID 18839948 DOI: 10.1021/Ja8052255 |
0.652 |
|
| 2008 |
Kovaleva EG, Lipscomb JD. Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. Biochemistry. 47: 11168-70. PMID 18826259 DOI: 10.1021/Bi801459Q |
0.478 |
|
| 2008 |
Mitić N, Schwartz JK, Brazeau BJ, Lipscomb JD, Solomon EI. CD and MCD studies of the effects of component B variant binding on the biferrous active site of methane monooxygenase. Biochemistry. 47: 8386-97. PMID 18627173 DOI: 10.1021/Bi800818W |
0.813 |
|
| 2008 |
Emerson JP, Kovaleva EG, Farquhar ER, Lipscomb JD, Que L. Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state. Proceedings of the National Academy of Sciences of the United States of America. 105: 7347-52. PMID 18492808 DOI: 10.1073/Pnas.0711179105 |
0.639 |
|
| 2008 |
Kovaleva EG, Lipscomb JD. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nature Chemical Biology. 4: 186-93. PMID 18277980 DOI: 10.1038/Nchembio.71 |
0.505 |
|
| 2008 |
Ohta T, Chakrabarty S, Lipscomb JD, Solomon EI. Near-IR MCD of the nonheme ferrous active site in naphthalene 1,2-dioxygenase: correlation to crystallography and structural insight into the mechanism of Rieske dioxygenases. Journal of the American Chemical Society. 130: 1601-10. PMID 18189388 DOI: 10.1021/Ja074769O |
0.668 |
|
| 2008 |
Pau MYM, Lipscomb JD, Solomon EI. Substrate activation for O2 reactions by oxidized metal centers in biology (Proceedings of the National Academy of Sciences of the United States of America (November 20, 2007) 104, 47, (18355-18362) doi:10.1073/pnas. 0704191104) Proceedings of the National Academy of Sciences of the United States of America. 105: 1098. DOI: 10.1073/Pnas.0711661105 |
0.377 |
|
| 2008 |
Lipscomb JD, Lee SK, Nesheim JC, Jin Y, Wallar BJ, Zhang XY. Intermediates in the reaction cycle of methane monooxygenase: Structure and chemistry Iron Metabolism: Inorganic Biochemistry and Regulatory Mechanisms. 323-339. DOI: 10.1002/9783527613700.ch19 |
0.711 |
|
| 2007 |
Pau MY, Lipscomb JD, Solomon EI. Substrate activation for O2 reactions by oxidized metal centers in biology. Proceedings of the National Academy of Sciences of the United States of America. 104: 18355-62. PMID 18003930 DOI: 10.1073/Pnas.0704191104 |
0.516 |
|
| 2007 |
Yan F, Moon SJ, Liu P, Zhao Z, Lipscomb JD, Liu A, Liu HW. Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues. Biochemistry. 46: 12628-38. PMID 17927218 DOI: 10.1021/Bi701370E |
0.636 |
|
| 2007 |
Yoon SS, Karabulut AC, Lipscomb JD, Hennigan RF, Lymar SV, Groce SL, Herr AB, Howell ML, Kiley PJ, Schurr MJ, Gaston B, Choi KH, Schweizer HP, Hassett DJ. Two-pronged survival strategy for the major cystic fibrosis pathogen, Pseudomonas aeruginosa, lacking the capacity to degrade nitric oxide during anaerobic respiration. The Embo Journal. 26: 3662-72. PMID 17627281 DOI: 10.1038/Sj.Emboj.7601787 |
0.784 |
|
| 2007 |
Neibergall MB, Stubna A, Mekmouche Y, Münck E, Lipscomb JD. Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidized benzoate 1,2-dioxygenase. Biochemistry. 46: 8004-16. PMID 17567152 DOI: 10.1021/Bi700120J |
0.84 |
|
| 2007 |
Kovaleva EG, Neibergall MB, Chakrabarty S, Lipscomb JD. Finding intermediates in the O2 activation pathways of non-heme iron oxygenases. Accounts of Chemical Research. 40: 475-83. PMID 17567087 DOI: 10.1021/Ar700052V |
0.825 |
|
| 2007 |
Brown CD, Neidig ML, Neibergall MB, Lipscomb JD, Solomon EI. VTVH-MCD and DFT studies of thiolate bonding to [FeNO]7/[FeO2]8 complexes of isopenicillin N synthase: substrate determination of oxidase versus oxygenase activity in nonheme Fe enzymes. Journal of the American Chemical Society. 129: 7427-38. PMID 17506560 DOI: 10.1021/Ja071364V |
0.832 |
|
| 2007 |
Kovaleva EG, Lipscomb JD. Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science (New York, N.Y.). 316: 453-7. PMID 17446402 DOI: 10.1126/Science.1134697 |
0.472 |
|
| 2007 |
Chakrabarty S, Austin RN, Deng D, Groves JT, Lipscomb JD. Radical intermediates in monooxygenase reactions of rieske dioxygenases. Journal of the American Chemical Society. 129: 3514-5. PMID 17341076 DOI: 10.1021/Ja068188V |
0.649 |
|
| 2007 |
Pau MY, Davis MI, Orville AM, Lipscomb JD, Solomon EI. Spectroscopic and electronic structure study of the enzyme-substrate complex of intradiol dioxygenases: substrate activation by a high-spin ferric non-heme iron site. Journal of the American Chemical Society. 129: 1944-58. PMID 17256852 DOI: 10.1021/Ja065671X |
0.487 |
|
| 2006 |
Zhang J, Wallar BJ, Popescu CV, Renner DB, Thomas DD, Lipscomb JD. Methane monooxygenase hydroxylase and B component interactions. Biochemistry. 45: 2913-26. PMID 16503646 DOI: 10.1021/Bi052256T |
0.753 |
|
| 2006 |
Zheng H, Lipscomb JD. Regulation of methane monooxygenase catalysis based on size exclusion and quantum tunneling. Biochemistry. 45: 1685-92. PMID 16460015 DOI: 10.1021/Bi051605G |
0.453 |
|
| 2006 |
Zhang J, Lipscomb JD. Role of the C-terminal region of the B component of Methylosinus trichosporium OB3b methane monooxygenase in the regulation of oxygen activation. Biochemistry. 45: 1459-69. PMID 16445288 DOI: 10.1021/Bi051721J |
0.44 |
|
| 2006 |
Zhang J, Zheng H, Groce SL, Lipscomb JD. Basis for specificity in methane monooxygenase and related non-heme iron-containing biological oxidation catalysts Journal of Molecular Catalysis a: Chemical. 251: 54-65. DOI: 10.1016/J.Molcata.2006.02.023 |
0.821 |
|
| 2005 |
Horsman GP, Jirasek A, Vaillancourt FH, Barbosa CJ, Jarzecki AA, Xu C, Mekmouche Y, Spiro TG, Lipscomb JD, Blades MW, Turner RF, Eltis LD. Spectroscopic studies of the anaerobic enzyme-substrate complex of catechol 1,2-dioxygenase. Journal of the American Chemical Society. 127: 16882-91. PMID 16316234 DOI: 10.1021/Ja053800O |
0.434 |
|
| 2005 |
Liu A, Jin Y, Zhang J, Brazeau BJ, Lipscomb JD. Substrate radical intermediates in soluble methane monooxygenase. Biochemical and Biophysical Research Communications. 338: 254-61. PMID 16165086 DOI: 10.1016/J.Bbrc.2005.08.216 |
0.797 |
|
| 2005 |
Yan F, Li T, Lipscomb JD, Liu A, Liu HW. Site-directed mutagenesis and spectroscopic studies of the iron-binding site of (S)-2-hydroxypropylphosphonic acid epoxidase. Archives of Biochemistry and Biophysics. 442: 82-91. PMID 16150418 DOI: 10.1016/J.Abb.2005.07.024 |
0.787 |
|
| 2005 |
Valley MP, Brown CK, Burk DL, Vetting MW, Ohlendorf DH, Lipscomb JD. Roles of the equatorial tyrosyl iron ligand of protocatechuate 3,4-dioxygenase in catalysis. Biochemistry. 44: 11024-39. PMID 16101286 DOI: 10.1021/Bi050902I |
0.798 |
|
| 2005 |
Lipscomb JD, Hoffman BM. Allosteric control of O2 reactivity in Rieske oxygenases. Structure (London, England : 1993). 13: 684-5. PMID 15893657 DOI: 10.1016/J.Str.2005.04.003 |
0.389 |
|
| 2005 |
Tierney DL, Rocklin AM, Lipscomb JD, Que L, Hoffman BM. ENDOR studies of the ligation and structure of the non-heme iron site in ACC oxidase. Journal of the American Chemical Society. 127: 7005-13. PMID 15884944 DOI: 10.1021/Ja0500862 |
0.659 |
|
| 2005 |
Groce SL, Lipscomb JD. Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates. Biochemistry. 44: 7175-88. PMID 15882056 DOI: 10.1021/Bi050180V |
0.818 |
|
| 2005 |
Hoeft RD, Groce SL, Lipscomb JD, Ohlendorf DH. Analysis of mutants of an active site base in a non-heme extradiol dioxygenase Acta Crystallographica Section a Foundations of Crystallography. 61: c210-c210. DOI: 10.1107/S0108767305091063 |
0.758 |
|
| 2004 |
Groce SL, Miller-Rodeberg MA, Lipscomb JD. Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase. Biochemistry. 43: 15141-53. PMID 15568806 DOI: 10.1021/Bi048690X |
0.827 |
|
| 2004 |
Vetting MW, Wackett LP, Que L, Lipscomb JD, Ohlendorf DH. Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. Journal of Bacteriology. 186: 1945-58. PMID 15028678 DOI: 10.1128/Jb.186.7.1945-1958.2004 |
0.618 |
|
| 2004 |
Rocklin AM, Kato K, Liu HW, Que L, Lipscomb JD. Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 171-82. PMID 14714198 DOI: 10.1007/S00775-003-0510-3 |
0.685 |
|
| 2003 |
Brazeau BJ, Wallar BJ, Lipscomb JD. Effector proteins from P450(cam) and methane monooxygenase: lessons in tuning nature's powerful reagents. Biochemical and Biophysical Research Communications. 312: 143-8. PMID 14630032 DOI: 10.1016/J.Bbrc.2003.09.242 |
0.798 |
|
| 2003 |
Liu P, Liu A, Yan F, Wolfe MD, Lipscomb JD, Liu HW. Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme. Biochemistry. 42: 11577-86. PMID 14529267 DOI: 10.1021/Bi030140W |
0.813 |
|
| 2003 |
Groce SL, Lipscomb JD. Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme. Journal of the American Chemical Society. 125: 11780-1. PMID 14505375 DOI: 10.1021/Ja0368103 |
0.828 |
|
| 2003 |
Yang TC, Wolfe MD, Neibergall MB, Mekmouche Y, Lipscomb JD, Hoffman BM. Substrate binding to NO-ferro-naphthalene 1,2-dioxygenase studied by high-resolution Q-band pulsed 2H-ENDOR spectroscopy. Journal of the American Chemical Society. 125: 7056-66. PMID 12783560 DOI: 10.1021/Ja0214126 |
0.806 |
|
| 2003 |
Brazeau BJ, Lipscomb JD. Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B. Biochemistry. 42: 5618-31. PMID 12741818 DOI: 10.1021/Bi027429I |
0.807 |
|
| 2003 |
Wasinger EC, Davis MI, Pau MY, Orville AM, Zaleski JM, Hedman B, Lipscomb JD, Hodgson KO, Solomon EI. Spectroscopic studies of the effect of ligand donor strength on the Fe-NO bond intradiol dioxygenases. Inorganic Chemistry. 42: 365-76. PMID 12693216 DOI: 10.1021/Ic025906F |
0.455 |
|
| 2003 |
Yang TC, Wolfe MD, Neibergall MB, Mekmouche Y, Lipscomb JD, Hoffman BM. Modulation of substrate binding to naphthalene 1,2-dioxygenase by rieske cluster reduction/oxidation. Journal of the American Chemical Society. 125: 2034-5. PMID 12590516 DOI: 10.1021/Ja028781M |
0.831 |
|
| 2003 |
Wolfe MD, Lipscomb JD. Hydrogen peroxide-coupled cis-diol formation catalyzed by naphthalene 1,2-dioxygenase. The Journal of Biological Chemistry. 278: 829-35. PMID 12403773 DOI: 10.1074/Jbc.M209604200 |
0.77 |
|
| 2002 |
Wolfe MD, Altier DJ, Stubna A, Popescu CV, Münck E, Lipscomb JD. Benzoate 1,2-dioxygenase from Pseudomonas putida: single turnover kinetics and regulation of a two-component Rieske dioxygenase. Biochemistry. 41: 9611-26. PMID 12135383 DOI: 10.1021/Bi025912N |
0.785 |
|
| 2002 |
Zhou J, Rocklin AM, Lipscomb JD, Que L, Solomon EI. Spectroscopic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: molecular mechanism and CO(2) activation in the biosynthesis of ethylene. Journal of the American Chemical Society. 124: 4602-9. PMID 11971707 DOI: 10.1021/Ja017250F |
0.688 |
|
| 2002 |
Davis MI, Orville AM, Neese F, Zaleski JM, Lipscomb JD, Solomon EI. Spectroscopic and electronic structure studies of protocatechuate 3,4-dioxygenase: nature of tyrosinate-Fe(III) bonds and their contribution to reactivity. Journal of the American Chemical Society. 124: 602-14. PMID 11804491 DOI: 10.1021/Ja011945Z |
0.461 |
|
| 2002 |
Lipscomb JD, Brazeau BJ, Wallar BJ. Methane monooxygenase and compound Q: lessons in oxygen activation International Congress Series. 1233: 205-212. DOI: 10.1016/S0531-5131(02)00278-9 |
0.764 |
|
| 2002 |
Brazeau BJ, Lipscomb JD. Thermodynamic and kinetic evidence for a two-step reaction between methane monooxygenase compound Q and substrates International Congress Series. 1233: 229-233. DOI: 10.1016/S0531-5131(02)00145-0 |
0.771 |
|
| 2001 |
Brazeau BJ, Austin RN, Tarr C, Groves JT, Lipscomb JD. Intermediate Q from soluble methane monooxygenase hydroxylates the mechanistic substrate probe norcarane: evidence for a stepwise reaction. Journal of the American Chemical Society. 123: 11831-7. PMID 11724588 DOI: 10.1021/Ja016376+ |
0.817 |
|
| 2001 |
Jin Y, Lipscomb JD. Desaturation reactions catalyzed by soluble methane monooxygenase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 717-25. PMID 11681705 DOI: 10.1007/S007750100250 |
0.519 |
|
| 2001 |
Brazeau BJ, Wallar BJ, Lipscomb JD. Unmasking of deuterium kinetic isotope effects on the methane monooxygenase compound Q reaction by site-directed mutagenesis of component B. Journal of the American Chemical Society. 123: 10421-2. PMID 11604007 DOI: 10.1021/Ja016632I |
0.784 |
|
| 2001 |
Chang SL, Wallar BJ, Lipscomb JD, Mayo KH. Residues in Methylosinus trichosporium OB3b methane monooxygenase component B involved in molecular interactions with reduced- and oxidized-hydroxylase component: a role for the N-terminus. Biochemistry. 40: 9539-51. PMID 11583153 DOI: 10.1021/Bi0103462 |
0.75 |
|
| 2001 |
Wallar BJ, Lipscomb JD. Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. Biochemistry. 40: 2220-33. PMID 11329291 DOI: 10.1021/Bi002298B |
0.757 |
|
| 2001 |
Wolfe MD, Parales JV, Gibson DT, Lipscomb JD. Single turnover chemistry and regulation of O2 activation by the oxygenase component of naphthalene 1,2-dioxygenase. The Journal of Biological Chemistry. 276: 1945-53. PMID 11056161 DOI: 10.1074/Jbc.M007795200 |
0.776 |
|
| 2000 |
Brazeau BJ, Lipscomb JD. Electron transfer and radical forming reactions of methane monooxygenase. Sub-Cellular Biochemistry. 35: 233-77. PMID 11192723 DOI: 10.1007/0-306-46828-X_7 |
0.808 |
|
| 2000 |
Jin Y, Lipscomb JD. Mechanistic insights into C-H activation from radical clock chemistry: oxidation of substituted methylcyclopropanes catalyzed by soluble methane monooxygenase from Methylosinus trichosporium OB3b. Biochimica Et Biophysica Acta. 1543: 47-59. PMID 11087940 DOI: 10.1016/S0167-4838(00)00199-0 |
0.496 |
|
| 2000 |
Brazeau BJ, Lipscomb JD. Kinetics and activation thermodynamics of methane monooxygenase compound Q formation and reaction with substrates. Biochemistry. 39: 13503-15. PMID 11063587 DOI: 10.1021/Bi001473L |
0.805 |
|
| 2000 |
Hassett DJ, Ochsner UA, Groce SL, Parvatiyar K, Ma JF, Lipscomb JD. Hydrogen peroxide sensitivity of catechol-2,3-dioxygenase: a cautionary note on use of xylE reporter fusions under aerobic conditions. Applied and Environmental Microbiology. 66: 4119-23. PMID 10966438 DOI: 10.1128/Aem.66.9.4119-4123.2000 |
0.768 |
|
| 1999 |
Davis MI, Wasinger EC, Westre TE, Zaleski JM, Orville AM, Lipscomb JD, Hedman B, Hodgson KO, Solomon EI. Spectroscopic Investigation of Reduced Protocatechuate 3,4-Dioxygenase: Charge-Induced Alterations in the Active Site Iron Coordination Environment. Inorganic Chemistry. 38: 3676-3683. PMID 11671125 DOI: 10.1021/Ic981464P |
0.408 |
|
| 1999 |
Rocklin AM, Tierney DL, Kofman V, Brunhuber NM, Hoffman BM, Christoffersen RE, Reich NO, Lipscomb JD, Que L. Role of the nonheme Fe(II) center in the biosynthesis of the plant hormone ethylene. Proceedings of the National Academy of Sciences of the United States of America. 96: 7905-9. PMID 10393920 DOI: 10.1073/Pnas.96.14.7905 |
0.52 |
|
| 1999 |
Jin Y, Lipscomb JD. Probing the mechanism of C-H activation: oxidation of methylcubane by soluble methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry. 38: 6178-86. PMID 10320346 DOI: 10.1021/Bi990068V |
0.52 |
|
| 1999 |
Chang SL, Wallar BJ, Lipscomb JD, Mayo KH. Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. Biochemistry. 38: 5799-812. PMID 10231531 DOI: 10.1021/Bi982992F |
0.726 |
|
| 1999 |
Lee SK, Lipscomb JD. Oxygen activation catalyzed by methane monooxygenase hydroxylase component: proton delivery during the O-O bond cleavage steps. Biochemistry. 38: 4423-32. PMID 10194363 DOI: 10.1021/Bi982712W |
0.403 |
|
| 1998 |
Frazee RW, Orville AM, Dolbeare KB, Yu H, Ohlendorf DH, Lipscomb JD. The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates. Biochemistry. 37: 2131-44. PMID 9485360 DOI: 10.1021/Bi972047B |
0.539 |
|
| 1998 |
Kauffmann KE, Popescu CV, Dong Y, Lipscomb JD, Que L, Münck E. Mossbauer evidence for antisymmetric exchange in a diferric synthetic complex and diferric methane monooxygenase Journal of the American Chemical Society. 120: 8739-8746. DOI: 10.1021/Ja981065T |
0.344 |
|
| 1998 |
Lipscomb JD, Que L. MMO: P450 in wolf's clothing? Journal of Biological Inorganic Chemistry. 3: 331-336. DOI: 10.1007/S007750050241 |
0.432 |
|
| 1998 |
Orville AM, Lipscomb JD, Ohlendorf DH. Probing the Reaction Mechanism of Protocatechuate 3,4-Dioxygenase with X-Ray Crystallography The Keio Journal of Medicine. 45: 282-288. DOI: 10.1007/978-4-431-68476-3_35 |
0.45 |
|
| 1998 |
Lipscomb JD, Orville AM, Frazee RW, Miller MA, Ohlendorf DH. Fundamentally Divergent Strategies for Oxygen Activation by Fe 2+ and Fe 3+ Catecholic Dioxygenases The Keio Journal of Medicine. 45: 263-275. DOI: 10.1007/978-4-431-68476-3_33 |
0.512 |
|
| 1997 |
Orville AM, Lipscomb JD. Cyanide and nitric oxide binding to reduced protocatechuate 3,4-dioxygenase: insight into the basis for order-dependent ligand binding by intradiol catecholic dioxygenases. Biochemistry. 36: 14044-55. PMID 9369476 DOI: 10.1021/Bi970609L |
0.431 |
|
| 1997 |
Elgren TE, Orville AM, Kelly KA, Lipscomb JD, Ohlendorf DH, Que L. Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate. Biochemistry. 36: 11504-13. PMID 9298971 DOI: 10.1021/Bi970691K |
0.443 |
|
| 1997 |
Orville AM, Lipscomb JD, Ohlendorf DH. Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding. Biochemistry. 36: 10052-66. PMID 9254600 DOI: 10.1021/Bi970469F |
0.492 |
|
| 1997 |
Orville AM, Elango N, Lipscomb JD, Ohlendorf DH. Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site. Biochemistry. 36: 10039-51. PMID 9254599 DOI: 10.1021/Bi970468N |
0.431 |
|
| 1997 |
Wang YZ, Lipscomb JD. Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. Protein Expression and Purification. 10: 1-9. PMID 9179284 DOI: 10.1006/Prep.1996.0703 |
0.36 |
|
| 1997 |
Liu Y, Nesheim JC, Paulsen KE, Stankovich MT, Lipscomb JD. Roles of the methane monooxygenase reductase component in the regulation of catalysis. Biochemistry. 36: 5223-33. PMID 9136884 DOI: 10.1021/Bi962743W |
0.472 |
|
| 1997 |
Elango N, Radhakrishnan R, Froland WA, Wallar BJ, Earhart CA, Lipscomb JD, Ohlendorf DH. Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b. Protein Science : a Publication of the Protein Society. 6: 556-68. PMID 9070438 DOI: 10.1002/Pro.5560060305 |
0.762 |
|
| 1997 |
Davydov A, Davydov R, Gräslund A, Lipscomb JD, Andersson KK. Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K. EPR evidence for conformational change upon reduction or binding of component B to the diferric state. The Journal of Biological Chemistry. 272: 7022-6. PMID 9054392 DOI: 10.1074/Jbc.272.11.7022 |
0.466 |
|
| 1997 |
Shu L, Nesheim JC, Kauffmann K, Münck E, Lipscomb JD, Que L. An Fe2IVO2 diamond core structure for the key intermediate Q of methane monooxygenase. Science (New York, N.Y.). 275: 515-8. PMID 8999792 DOI: 10.1126/Science.275.5299.515 |
0.489 |
|
| 1997 |
Pulver SC, Froland WA, Lipscomb JD, Solomon EI. Ligand field circular dichroism and magnetic circular dichroism studies of component B and substrate binding to the hydroxylase component of methane monooxygenase Journal of the American Chemical Society. 119: 387-395. DOI: 10.1021/Ja962854I |
0.305 |
|
| 1997 |
Lipscomb J, Nesheim J, Lee S, Wallar B, Zhang X. Structure and reactivity of intermediates in the oxygen activation mechanism of methane monooxygenase Journal of Inorganic Biochemistry. 67: 314. DOI: 10.1016/S0162-0134(97)80183-3 |
0.73 |
|
| 1997 |
Wolfe MD, Altier DJ, Lipscomb JD. Spectroscopic characterization of substrate binding to the oxygenase component of benzoate 1,2-dioxygenase Faseb Journal. 11: A1303. |
0.68 |
|
| 1996 |
Wallar BJ, Lipscomb JD. Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters. Chemical Reviews. 96: 2625-2658. PMID 11848839 DOI: 10.1021/Cr9500489 |
0.756 |
|
| 1996 |
Nesheim JC, Lipscomb JD. Large kinetic isotope effects in methane oxidation catalyzed by methane monooxygenase: evidence for C-H bond cleavage in a reaction cycle intermediate. Biochemistry. 35: 10240-7. PMID 8756490 DOI: 10.1021/Bi960596W |
0.396 |
|
| 1996 |
Miller MA, Lipscomb JD. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity. The Journal of Biological Chemistry. 271: 5524-35. PMID 8621411 DOI: 10.1074/Jbc.271.10.5524 |
0.543 |
|
| 1996 |
Shu L, Liu Y, Lipscomb JD, Que L. X-ray absorption spectroscopic studies of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b Journal of Biological Inorganic Chemistry. 1: 297-304. DOI: 10.1007/S007750050057 |
0.422 |
|
| 1995 |
Shu L, Chiou YM, Orville AM, Miller MA, Lipscomb JD, Que L. X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism. Biochemistry. 34: 6649-59. PMID 7756296 DOI: 10.1021/Bi00020A010 |
0.493 |
|
| 1995 |
Liu Y, Nesheim JC, Lee SK, Lipscomb JD. Gating effects of component B on oxygen activation by the methane monooxygenase hydroxylase component. The Journal of Biological Chemistry. 270: 24662-5. PMID 7559577 DOI: 10.1074/Jbc.270.42.24662 |
0.422 |
|
| 1995 |
Liu Y, Nesheim J, Paulsen K, Wallar B, Stankovich M, Lipscomb J. Roles of component B and reductase in methane monooxygenase (MMO) turnover Journal of Inorganic Biochemistry. 59: 368. DOI: 10.1016/0162-0134(95)97466-4 |
0.697 |
|
| 1995 |
Orville AM, Elango N, Ohlendorf DH, Lipscomb JD. Crystal structures of substrate & substrate analog complexes of protocatechuate 3,4-dioxygenase yield mechanistic insights Journal of Inorganic Biochemistry. 59: 367. DOI: 10.1016/0162-0134(95)97465-3 |
0.323 |
|
| 1995 |
Frazee R, Yu H, Dolbeare K, Lipscomb J. Mutations of Tyr447 in protocatechuate 3,4-dioxygenase: Role of the displaceable iron ligand Journal of Inorganic Biochemistry. 59: 366. DOI: 10.1016/0162-0134(95)97464-2 |
0.309 |
|
| 1995 |
Zaleski JM, Loeb KE, Orville AM, Kappock T, Caradonna JP, Lipscomb JD, Solomon EI. Structure/function relationships in mononuclear non-heme iron enzymes Journal of Inorganic Biochemistry. 59: 364. DOI: 10.1016/0162-0134(95)97462-Y |
0.372 |
|
| 1994 |
Paulsen KE, Liu Y, Fox BG, Lipscomb JD, Münck E, Stankovich MT. Oxidation-reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b. Biochemistry. 33: 713-22. PMID 8292599 DOI: 10.1021/Bi00169A013 |
0.644 |
|
| 1994 |
Ohlendorf DH, Orville AM, Lipscomb JD. Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution. Journal of Molecular Biology. 244: 586-608. PMID 7990141 DOI: 10.1006/Jmbi.1994.1754 |
0.341 |
|
| 1994 |
Lipscomb JD. Biochemistry of the soluble methane monooxygenase. Annual Review of Microbiology. 48: 371-99. PMID 7826011 DOI: 10.1146/Annurev.Mi.48.100194.002103 |
0.524 |
|
| 1994 |
Hendrich MP, Logan M, Andersson KK, Arciero DM, Lipscomb JD, Hooper AB. The active site of hydroxylamine oxidoreductase from nitrosomonas: Evidence for a new metal cluster in enzymes Journal of the American Chemical Society. 116: 11961-11968. DOI: 10.1021/Ja00105A041 |
0.379 |
|
| 1994 |
Pulver S, Froland WA, Fox BG, Lipscomb JD, Solomon EI. Spectroscopic studies of the coupled binuclear non-heme iron active site in the fully reduced hydroxylase component of methane monooxygenase: comparison to deoxy and deoxy-azide hemerythrin. [Erratum to document cited in CA120:3498] Journal of the American Chemical Society. 116: 4529-4529. DOI: 10.1021/Ja00089A077 |
0.585 |
|
| 1993 |
Lee SK, Nesheim JC, Lipscomb JD. Transient intermediates of the methane monooxygenase catalytic cycle. The Journal of Biological Chemistry. 268: 21569-77. PMID 8408008 |
0.323 |
|
| 1993 |
Frazee RW, Livingston DM, LaPorte DC, Lipscomb JD. Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes. Journal of Bacteriology. 175: 6194-202. PMID 8407791 DOI: 10.1128/Jb.175.19.6194-6202.1993 |
0.309 |
|
| 1993 |
Wolgel SA, Dege JE, Perkins-Olson PE, Jaurez-Garcia CH, Crawford RL, Münck E, Lipscomb JD. Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: a new extradiol catecholic dioxygenase. Journal of Bacteriology. 175: 4414-26. PMID 8392511 DOI: 10.1128/Jb.175.14.4414-4426.1993 |
0.512 |
|
| 1993 |
Orville AM, Lipscomb JD. Simultaneous binding of nitric oxide and isotopically labeled substrates or inhibitors by reduced protocatechuate 3,4-dioxygenase. The Journal of Biological Chemistry. 268: 8596-607. PMID 8386164 |
0.392 |
|
| 1993 |
Pulver S, Froland WA, Fox BG, Lipscomb JD, Solomon EI. Spectroscopic studies of the coupled binuclear non-heme iron active site in the fully reduced hydroxylase component of methane monooxygenase: Comparison to deoxy and deoxy-azide hemerythrin Journal of the American Chemical Society. 115: 12409-12422. DOI: 10.1021/Ja00079A024 |
0.613 |
|
| 1993 |
Thomann H, Bernardo M, McCormick JM, Pulver S, Andersson KK, Lipscomb JD, Solomon EI. Pulsed EPR studies of mixed valent [Fe(II)Fe(III)] forms of hemerythrin and methane monooxygenase: evidence for a hydroxide bridge Journal of the American Chemical Society. 115: 8881-8882. DOI: 10.1021/Ja00072A068 |
0.383 |
|
| 1993 |
Lee SK, Fox BG, Froland WA, Lipscomb JD, Münck E. A transient intermediate of the methane monooxygenase catalytic cycle containing an FeIVFeIV cluster Journal of the American Chemical Society. 115: 6450-6451. DOI: 10.1021/Ja00067A086 |
0.545 |
|
| 1993 |
Fox BG, Hendrich MP, Surerus KK, Andersson KK, Froland WA, Lipscomb JD, Munck E. Moessbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b Journal of the American Chemical Society. 115: 3688-3701. DOI: 10.1021/Ja00062A039 |
0.601 |
|
| 1993 |
Miller MA, Lipscomb JD. Homoprotocatechuate 2,3-dioxygenase purified from Brevibacterium fuscum: An Fe(II) dioxygenase Journal of Inorganic Biochemistry. 51: 301. DOI: 10.1016/0162-0134(93)85333-4 |
0.371 |
|
| 1993 |
Altier DJ, Fox BG, Münck E, Lipscomb JD. EPR And Mössbauer characterization of benzoate 1,2-dioxygenase from P. putida Journal of Inorganic Biochemistry. 51: 300. DOI: 10.1016/0162-0134(93)85332-3 |
0.512 |
|
| 1993 |
Andersson K, Elgren T, Fox B, Hendrich M, Froland W, Münck E, Que L, Lipscomb J. Binding of phenols to the diiron cluster of soluble methane monooxygenase hydroxylase component. Journal of Inorganic Biochemistry. 51: 299. DOI: 10.1016/0162-0134(93)85331-2 |
0.544 |
|
| 1993 |
Orville AM, Lipscomb JD, Ohlendorf DH. Alteration in the iron ligand structure of protocatechuate 3,4-dioxygenase (3,4-PCD) in response to exogenous ligand binding Journal of Inorganic Biochemistry. 51: 295. DOI: 10.1016/0162-0134(93)85327-5 |
0.325 |
|
| 1993 |
Froland WA, Priestley ND, Floss HG, Williams PG, Morimoto H, Lipscomb JD. Evidence supporting the formation of a substrate radical during H2O2-coupled MMO catalyzed oxidation of chiral ethane Journal of Inorganic Biochemistry. 51: 245. DOI: 10.1016/0162-0134(93)85279-H |
0.359 |
|
| 1993 |
Lee S, Fox BG, Nesheim JC, Froland WA, Münck E, Lipscomb JD. Stabilization and characterization of a reactive Fe(IV)·Fe(IV) intermediate of methane monooxygenase catalytic cycle Journal of Inorganic Biochemistry. 51: 243. DOI: 10.1016/0162-0134(93)85277-F |
0.614 |
|
| 1993 |
Lipscomb J, Lee S, Froland W, Liu Y, Nesheim J, Andersson K. Reaction cycle chemistry of soluble methane monooxygenase (MMO) Journal of Inorganic Biochemistry. 51: 242. DOI: 10.1016/0162-0134(93)85276-E |
0.32 |
|
| 1993 |
Pulver S, Martin Bollinger J, Froland WA, Lipscomb JD, Stubbe J, Solomon EI. Structure-function correlations over coupled binuclear non-heme iron enzymes Journal of Inorganic Biochemistry. 51: 63. DOI: 10.1016/0162-0134(93)85099-T |
0.373 |
|
| 1992 |
Siu DC, Orville AM, Lipscomb JD, Ohlendorf DH, Que L. Resonance Raman studies of the protocatechuate 3,4-dioxygenase from Brevibacterium fuscum. Biochemistry. 31: 10443-8. PMID 1420163 DOI: 10.1021/Bi00158A005 |
0.392 |
|
| 1992 |
Paulsen KE, Orville AM, Frerman FE, Lipscomb JD, Stankovich MT. Redox properties of electron-transfer flavoprotein ubiquinone oxidoreductase as determined by EPR-spectroelectrochemistry. Biochemistry. 31: 11755-61. PMID 1332770 DOI: 10.1021/Bi00162A012 |
0.339 |
|
| 1992 |
Froland WA, Andersson KK, Lee SK, Liu Y, Lipscomb JD. Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed reactions. A novel role for protein-protein interactions in an oxygenase mechanism. The Journal of Biological Chemistry. 267: 17588-97. PMID 1325441 |
0.339 |
|
| 1992 |
Orville AM, Chen VJ, Kriauciunas A, Harpel MR, Fox BG, Münck E, Lipscomb JD. Thiolate ligation of the active site Fe2+ of isopenicillin N synthase derives from substrate rather than endogenous cysteine: spectroscopic studies of site-specific Cys----Ser mutated enzymes. Biochemistry. 31: 4602-12. PMID 1316153 DOI: 10.1021/Bi00134A010 |
0.655 |
|
| 1992 |
Hendrich MP, Fox BG, Andersson KK, Debrunner PG, Lipscomb JD. Ligation of the diiron site of the hydroxylase component of methane monooxygenase. An electron nuclear double resonance study. The Journal of Biological Chemistry. 267: 261-9. PMID 1309736 |
0.591 |
|
| 1992 |
Andersson KK, Elgren TE, Que L, Lipscomb JD. Accessibility to the active site of methane monooxygenase: The first demonstration of exogenous ligand binding to the diiron cluster Journal of the American Chemical Society. 114: 8711-8713. DOI: 10.1021/Ja00048A061 |
0.346 |
|
| 1992 |
Priestley ND, Floss HG, Froland WA, Lipscomb JD, Williams PG, Morimoto H. Cryptic stereospecificity of methane monooxygenase Journal of the American Chemical Society. 114: 7561-7562. DOI: 10.1021/Ja00045A037 |
0.419 |
|
| 1991 |
Fox BG, Liu Y, Dege JE, Lipscomb JD. Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction. The Journal of Biological Chemistry. 266: 540-50. PMID 1845980 |
0.582 |
|
| 1991 |
Mabrouk PA, Orville AM, Lipscomb JD, Solomon EI. Variable-Temperature Variable-Field Magnetic Circular Dichroism Studies of the Fe(II) Active Site in Metapyrocatechase: Implications for the Molecular Mechanism of Extradiol Dioxygenases Journal of the American Chemical Society. 113: 4053-4061. DOI: 10.1021/Ja00011A001 |
0.343 |
|
| 1991 |
Orville A, Harpel M, Chen V, Kriauciunas A, Fox B, Srivastava K, Münck E, Lipscomb J. Substrate coordination to the active site Fe2+ of isopenicillin N synthase. Journal of Inorganic Biochemistry. 43: 558. DOI: 10.1016/0162-0134(91)84533-F |
0.621 |
|
| 1991 |
Hendrich MP, Fox BG, Andersson KK, Debrunner PG, Lipscomb JD. Ligation of the diiron site of the hydroxylase component of methane monooxygenase: An endor study. Journal of Inorganic Biochemistry. 43: 548. DOI: 10.1016/0162-0134(91)84523-C |
0.548 |
|
| 1990 |
Whittaker JW, Orville AM, Lipscomb JD. Protocatechuate 3,4-dioxygenase from Brevibacterium fuscum. Methods in Enzymology. 188: 82-8. PMID 2280720 DOI: 10.1016/0076-6879(90)88016-4 |
0.332 |
|
| 1990 |
Fox BG, Froland WA, Jollie DR, Lipscomb JD. Methane monooxygenase from Methylosinus trichosporium OB3b. Methods in Enzymology. 188: 191-202. PMID 2280705 DOI: 10.1016/0076-6879(90)88033-7 |
0.512 |
|
| 1990 |
Orville AM, Harpel MR, Lipscomb JD. Synthesis of 17O- or 18O-enriched dihydroxy aromatic compounds. Methods in Enzymology. 188: 107-15. PMID 2280695 DOI: 10.1016/0076-6879(90)88020-B |
0.314 |
|
| 1990 |
True AE, Orville AM, Pearce LL, Lipscomb JD, Que L. An EXAFS study of the interaction of substrate with the ferric active site of protocatechuate 3,4-dioxygenase. Biochemistry. 29: 10847-54. PMID 2271684 DOI: 10.1021/Bi00500A019 |
0.502 |
|
| 1990 |
Harpel MR, Lipscomb JD. Gentisate 1,2-dioxygenase from Pseudomonas. Substrate coordination to active site Fe2+ and mechanism of turnover. The Journal of Biological Chemistry. 265: 22187-96. PMID 2266121 |
0.401 |
|
| 1990 |
Fox BG, Borneman JG, Wackett LP, Lipscomb JD. Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: mechanistic and environmental implications. Biochemistry. 29: 6419-27. PMID 2207083 DOI: 10.1021/Bi00479A013 |
0.604 |
|
| 1990 |
Harpel MR, Lipscomb JD. Gentisate 1,2-dioxygenase from pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans. The Journal of Biological Chemistry. 265: 6301-11. PMID 2156846 |
0.386 |
|
| 1990 |
Jollie DR, Lipscomb JD. Formate dehydrogenase from Methylosinus trichosporium OB3b. Methods in Enzymology. 188: 331-4. PMID 2126333 DOI: 10.1016/0076-6879(90)88051-B |
0.431 |
|
| 1990 |
Hendrich MP, Münck E, Fox BG, Lipscomb JD. Integer-spin EPR studies of the fully reduced methane monooxygenase hydroxylase component Journal of the American Chemical Society. 112: 5861-5865. DOI: 10.1021/Ja00171A029 |
0.51 |
|
| 1989 |
Chen VJ, Orville AM, Harpel MR, Frolik CA, Surerus KK, Münck E, Lipscomb JD. Spectroscopic studies of isopenicillin N synthase. A mononuclear nonheme Fe2+ oxidase with metal coordination sites for small molecules and substrate. The Journal of Biological Chemistry. 264: 21677-81. PMID 2557336 |
0.413 |
|
| 1989 |
Fox BG, Froland WA, Dege JE, Lipscomb JD. Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph. The Journal of Biological Chemistry. 264: 10023-33. PMID 2542319 |
0.617 |
|
| 1989 |
Orville AM, Lipscomb JD. Binding of isotopically labeled substrates, inhibitors, and cyanide by protocatechuate 3,4-dioxygenase. The Journal of Biological Chemistry. 264: 8791-801. PMID 2542290 |
0.395 |
|
| 1989 |
Fox B, Lipscomb J, Surerus K, Hendrich M, Münck E. Spectroscopic studies of the methane monooxygenase from Methylosinus trichosporium OB3b Journal of Inorganic Biochemistry. 36: 322. DOI: 10.1016/0162-0134(89)84513-1 |
0.536 |
|
| 1988 |
Ohlendorf DH, Lipscomb JD, Weber PC. Structure and assembly of protocatechuate 3,4-dioxygenase. Nature. 336: 403-5. PMID 3194022 DOI: 10.1038/336403A0 |
0.37 |
|
| 1988 |
Fox BG, Lipscomb JD. Purification of a high specific activity methane monooxygenase hydroxylase component from a type II methanotroph. Biochemical and Biophysical Research Communications. 154: 165-70. PMID 2840063 DOI: 10.1016/0006-291X(88)90665-1 |
0.608 |
|
| 1988 |
Fox BG, Surerus KK, Münck E, Lipscomb JD. Evidence for a mu-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Mössbauer and EPR studies. The Journal of Biological Chemistry. 263: 10553-6. PMID 2839495 |
0.585 |
|
| 1987 |
Ohlendorf DH, Weber PC, Lipscomb JD. Determination of the quaternary structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. Journal of Molecular Biology. 195: 225-7. PMID 3116260 DOI: 10.1016/0022-2836(87)90340-8 |
0.301 |
|
| 1986 |
Arciero DM, Lipscomb JD. Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases. The Journal of Biological Chemistry. 261: 2170-8. PMID 3003098 |
0.413 |
|
| 1985 |
Arciero DM, Orville AM, Lipscomb JD. [17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases. The Journal of Biological Chemistry. 260: 14035-44. PMID 2997190 |
0.411 |
|
| 1985 |
DiSpirito AA, Taaffe LR, Lipscomb JD, Hooper AB. A 'blue' copper oxidase from Nitrosomonas europaea Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 827: 320-326. DOI: 10.1016/0167-4838(85)90217-1 |
0.344 |
|
| 1984 |
Whittaker JW, Lipscomb JD. 17O-water and cyanide ligation by the active site iron of protocatechuate 3,4-dioxygenase. Evidence for displaceable ligands in the native enzyme and in complexes with inhibitors or transition state analogs. The Journal of Biological Chemistry. 259: 4487-95. PMID 6323476 |
0.427 |
|
| 1984 |
Whittaker JW, Lipscomb JD. Transition state analogs for protocatechuate 3,4-dioxygenase. Spectroscopic and kinetic studies of the binding reactions of ketonized substrate analogs. The Journal of Biological Chemistry. 259: 4476-86. PMID 6323475 |
0.392 |
|
| 1984 |
Whittaker JW, Lipscomb JD, Kent TA, Münck E. Brevibacterium fuscum protocatechuate 3,4-dioxygenase. Purification, crystallization, and characterization. The Journal of Biological Chemistry. 259: 4466-75. PMID 6323474 |
0.358 |
|
| 1983 |
Arciero DM, Lipscomb JD, Huynh BH, Kent TA, Münck E. EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment. The Journal of Biological Chemistry. 258: 14981-91. PMID 6317682 |
0.406 |
|
| 1983 |
Whittaker J, Lipscomb J. Active site Fe3+ ligation by substrate and transition state analogs of protocatechuate 3,4 dioxygenase Inorganica Chimica Acta. 79: 210-211. DOI: 10.1016/S0020-1693(00)95243-5 |
0.47 |
|
| 1983 |
Andersson KK, Lipscomb JD, Hooper AB. Unusual spin interactions in the 24 heme hydroxylamine oxidoreductase and diheme cytochrome c 554 from nitrosomonas Inorganica Chimica Acta. 79: 181-182. DOI: 10.1016/S0020-1693(00)95215-0 |
0.365 |
|
| 1982 |
Kent TA, Moura I, Moura JJG, Lipscomb JD, Huynh BH, LeGall J, Xavier AV, Münck E. Conversion of [3 Fe3 S] into [4 Fe4 S] clusters in a Desulfovibrio gigas ferredoxin and isotopic labeling of iron-sulfur cluster subsites Febs Letters. 138: 55-58. DOI: 10.1016/0014-5793(82)80393-1 |
0.383 |
|
| 1980 |
Lipscomb JD. Electron paramagnetic resonance detectable states of cytochrome P-450cam. Biochemistry. 19: 3590-9. PMID 6250573 DOI: 10.1021/Bi00556A027 |
0.345 |
|
| 1978 |
Lipscomb JD, Harrison JE, Dus KM, Gunsalus IC. Cytochrome P450 cam: SS- dimer and -SH derivative reactivities. Biochemical and Biophysical Research Communications. 83: 771-8. PMID 213068 DOI: 10.1016/0006-291X(78)91461-4 |
0.605 |
|
| 1977 |
Que L, Lipscomb JD, Münck E, Wood JM. Protocatechuate 3,4-dioxygenase. Inhibitor studies and mechanistic implications. Biochimica Et Biophysica Acta. 485: 60-74. PMID 199266 DOI: 10.1016/0005-2744(77)90193-0 |
0.423 |
|
| 1976 |
Que L, Lipscomb JD, Zimmermann R, Münck E, Orme-Johnson NR, Orme-Johnson WH. Mössbauer and EPR spectroscopy of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. Biochimica Et Biophysica Acta. 452: 320-34. PMID 188463 DOI: 10.1016/0005-2744(76)90182-0 |
0.439 |
|
| 1976 |
Lipscomb JD, Sligar SG, Namtvedt MJ, Gunsalus IC. Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam. The Journal of Biological Chemistry. 251: 1116-24. PMID 2601 |
0.573 |
|
| 1976 |
Sharrock M, Debrunner PG, Schulz C, Lipscomb JD, Marshall V, Gunsalus IC. Cytochrome P450cam and its complexes. Mössbauer parameters of the heme iron. Biochimica Et Biophysica Acta. 420: 8-26. PMID 2296 DOI: 10.1016/0005-2795(76)90340-8 |
0.605 |
|
| 1976 |
MÜNCK E, ZIMMERMANN R, LIPSCOMB JD, QUE L, ORME-JOHNSON WH. CHARACTERIZATION OF AN OXYGENATED INTERMEDIATE IN A DIOXYGENASE REACTION BY EPR AND MÖSSBAUER SPECTROSCOPY Le Journal De Physique Colloques. 37: C6-203-C6-207. DOI: 10.1051/Jphyscol:1976643 |
0.453 |
|
| 1975 |
Champion PM, Lipscomb JD, Münck E, Debrunner P, Gunsalus IC. Mössbauer investigations of high-spin ferrous heme proteins. I. Cytochrome P-450. Biochemistry. 14: 4151-8. PMID 1182094 |
0.503 |
|
| 1975 |
Champion PM, Munck E, Debrunner PG, Moss TH, Lipscomb JD, Gunsalus IC. The magnetic susceptibility of reduced cytochrome P-450-cam. Biochimica Et Biophysica Acta. 376: 579-82. PMID 1125223 DOI: 10.1016/0005-2728(75)90179-6 |
0.561 |
|
| 1974 |
Sligar SG, Debrunner PG, Lipscomb JD, Namtvedt MJ, Gunsalus IC. A role of the putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations. Proceedings of the National Academy of Sciences of the United States of America. 71: 3906-10. PMID 4530269 DOI: 10.1073/Pnas.71.10.3906 |
0.557 |
|
| 1974 |
Sligar SG, Lipscomb JD, Debrunner PG, Gunsalus IC. Superoxide anion production by the autoxidation of cytochrome P450cam. Biochemical and Biophysical Research Communications. 61: 290-6. PMID 4441397 DOI: 10.1016/0006-291X(74)90565-8 |
0.548 |
|
| 1973 |
Sharrock M, Münck E, Debrunner PG, Marshall V, Lipscomb JD, Gunsalus IC. Mössbauer studies of cytochrome P-450 cam . Biochemistry. 12: 258-65. PMID 4682999 DOI: 10.1021/Bi00726A013 |
0.514 |
|
| 1973 |
Gunsalus IC, Meeks JR, Lipscomb JD. Cytochrome P-450cam substrate and effector interactions. Annals of the New York Academy of Sciences. 212: 107-21. PMID 4532472 |
0.477 |
|
| 1973 |
Lipscomb JD, Gunsalus IC. Structural aspects of the active site of cytochrome P-450cam. Drug Metabolism and Disposition: the Biological Fate of Chemicals. 1: 1-5. PMID 4149384 |
0.508 |
|
| 1972 |
Gunsalus IC, Lipscomb JD, Marshall V, Frauenfelder H, Greenbaum E, Münck E. Structure and reactions of oxygenase active centers: cytochrome P-450 and iron sulfur proteins. Biochemical Society Symposium. 34: 135-57. PMID 4348063 |
0.558 |
|
| 1972 |
Tyson CA, Lipscomb JD, Gunsalus IC. The role of putidaredoxin and P450 cam in methylene hydroxylation. The Journal of Biological Chemistry. 247: 5777-84. PMID 4341491 |
0.442 |
|
| 1971 |
Gunsalus IC, Tyson CA, Tsai R, Lipscomb JD. P-450cam hydroxylase: substrate-effector and electron-transport reactions Chemico-Biological Interactions. 4: 75-78. PMID 5156338 DOI: 10.1016/0009-2797(71)90036-6 |
0.55 |
|
| 1971 |
Gunsalus IC, Lipscomb JD, Marshall V, Frauenfelder H, Münck E, Greenbaum E. Structure and reactions of oxygenase active centres: cytochrome P-450 and iron-sulphur proteins. The Biochemical Journal. 125: 5P-6P. PMID 4335694 DOI: 10.1042/Bj1250005P |
0.601 |
|
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