| Year |
Citation |
Score |
| 2023 |
Quaye JA, Ouedraogo D, Gadda G. Targeted Mutation of a Non-catalytic Gating Residue Increases the Rate of d-Arginine Dehydrogenase Catalytic Turnover. Journal of Agricultural and Food Chemistry. 71: 17343-52. PMID 37933126 DOI: 10.1021/acs.jafc.3c05328 |
0.375 |
|
| 2023 |
Moni BM, Quaye JA, Gadda G. Mutation of a Distal Gating Residue Modulates NADH Binding in NADH:Quinone Oxidoreductase from Pseudomonas aeruginosa PAO1. The Journal of Biological Chemistry. 103044. PMID 36803963 DOI: 10.1016/j.jbc.2023.103044 |
0.45 |
|
| 2023 |
Ouedraogo D, Souffrant M, Yao XQ, Hamelberg D, Gadda G. Non-active Site Residue in Loop L4 Alters Substrate Capture and Product Release in d-Arginine Dehydrogenase. Biochemistry. PMID 36795942 DOI: 10.1021/acs.biochem.2c00697 |
0.394 |
|
| 2023 |
Quaye JA, Gadda G. The Pseudomonas aeruginosa PAO1 metallo flavoprotein D-2-hydroxyglutarate dehydrogenase requires Zn for substrate orientation and activation. The Journal of Biological Chemistry. 103008. PMID 36775127 DOI: 10.1016/j.jbc.2023.103008 |
0.451 |
|
| 2023 |
Quaye JA, Gadda G. Uncovering Zn as a cofactor of FAD-dependent Pseudomonas aeruginosa PAO1 D-2-hydroxyglutarate dehydrogenase. The Journal of Biological Chemistry. 103007. PMID 36775126 DOI: 10.1016/j.jbc.2023.103007 |
0.428 |
|
| 2022 |
Quaye JA, Ball J, Gadda G. Kinetic solvent viscosity effects uncover an internal isomerization of the enzyme-substrate complex in Pseudomonas aeruginosa PAO1 NADH:Quinone oxidoreductase. Archives of Biochemistry and Biophysics. 109342. PMID 35777523 DOI: 10.1016/j.abb.2022.109342 |
0.391 |
|
| 2021 |
Iyer A, Reis RAG, Gannavaram S, Momin M, Spring-Connell AM, Orozco-Gonzalez Y, Agniswamy J, Hamelberg D, Weber IT, Gozem S, Wang S, Germann MW, Gadda G. A Single-Point Mutation in d-Arginine Dehydrogenase Unlocks a Transient Conformational State Resulting in Altered Cofactor Reactivity. Biochemistry. PMID 33630571 DOI: 10.1021/acs.biochem.1c00054 |
0.466 |
|
| 2020 |
Quaye JA, Gadda G. Kinetic and Bioinformatic Characterization of d-2-Hydroxyglutarate Dehydrogenase from PAO1. Biochemistry. PMID 33301690 DOI: 10.1021/acs.biochem.0c00832 |
0.485 |
|
| 2020 |
Vodovoz M, Gadda G. Kinetic solvent viscosity effects reveal a protein isomerization in the reductive half-reaction of Neurospora crassa class II nitronate monooxygenase. Archives of Biochemistry and Biophysics. 108625. PMID 33038312 DOI: 10.1016/j.abb.2020.108625 |
0.441 |
|
| 2020 |
Gadda G. Choline oxidases. The Enzymes. 47: 137-166. PMID 32951822 DOI: 10.1016/bs.enz.2020.05.004 |
0.506 |
|
| 2020 |
Su D, Smitherman C, Gadda G. A Metastable Photoinduced Protein-Flavin Adduct in Choline Oxidase, an Enzyme not Involved in Light-Dependent Processes. The Journal of Physical Chemistry. B. PMID 32310661 DOI: 10.1021/Acs.Jpcb.0C02633 |
0.475 |
|
| 2019 |
Su D, Aguillon C, Gadda G. Characterization of conserved active site residues in class I nitronate monooxygenase. Archives of Biochemistry and Biophysics. PMID 31356775 DOI: 10.1016/J.Abb.2019.07.023 |
0.594 |
|
| 2019 |
Almeida Garcia Reis R, Salvi F, WIlliams I, Gadda G. Kinetic Investigation of a Presumed Nitronate Monooxygenase from Pseudomonas aeruginosa PAO1 Establishes a New Class of NAD(P)H:quinone Reductases. Biochemistry. PMID 31075192 DOI: 10.1021/Acs.Biochem.9B00207 |
0.567 |
|
| 2019 |
Francis K, Gadda G. On the use of noncompetitive kinetic isotope effects to investigate flavoenzyme mechanism. Methods in Enzymology. 620: 115-143. PMID 31072484 DOI: 10.1016/Bs.Mie.2019.03.008 |
0.526 |
|
| 2018 |
Ball J, Gannavaram S, Gadda G. Structural determinants for substrate specificity of flavoenzymes oxidizing d-amino acids. Archives of Biochemistry and Biophysics. PMID 30312594 DOI: 10.1016/J.Abb.2018.10.002 |
0.434 |
|
| 2018 |
Ball J, Reis RAG, Agniswamy J, Weber IT, Gadda G. STERIC HINDRANCE CONTROLS PYRIDINE NUCLEOTIDE SPECIFICITY OF A FLAVIN-DEPENDENT NADH:QUINONE OXIDOREDUCTASE. Protein Science : a Publication of the Protein Society. PMID 30246917 DOI: 10.1002/Pro.3514 |
0.48 |
|
| 2018 |
Robbins JM, Geng J, Barry BA, Gadda G, Bommarius AS. Photo-Irradiation Generates an Ultra-Stable 8-formyl FAD Semiquinone Radical with Unusual Properties in Formate Oxidase. Biochemistry. PMID 30226367 DOI: 10.1021/Acs.Biochem.8B00571 |
0.433 |
|
| 2018 |
Gadda G, Sobrado P. Kinetic Solvent Viscosity Effects as Probes to Study the Mechanisms of Enzyme Action. Biochemistry. PMID 29874467 DOI: 10.1021/Acs.Biochem.8B00232 |
0.731 |
|
| 2018 |
Flores E, Gadda G. Kinetic Characterization of PA1225 from Pseudomonas aeruginosa PAO1 Reveals a New NADPH:Quinone Reductase. Biochemistry. PMID 29715013 DOI: 10.1021/Acs.Biochem.8B00090 |
0.585 |
|
| 2018 |
Carro J, Ferreira P, Martínez AT, Gadda G. Stepwise Hydrogen Atom and Proton Transfers in Dioxygen Reduction by Aryl-Alcohol Oxidase. Biochemistry. PMID 29485859 DOI: 10.1021/Acs.Biochem.8B00106 |
0.512 |
|
| 2018 |
Robbins JM, Bommarius AS, Gadda G. Mechanistic studies of formate oxidase from Aspergillus oryzae: A novel member of the glucose-Methanol-choline oxidoreductase enzyme superfamily that oxidizes carbon acids. Archives of Biochemistry and Biophysics. PMID 29458006 DOI: 10.1016/J.Abb.2018.02.007 |
0.54 |
|
| 2018 |
Agniswamy J, Reis RAG, Wang YF, Smitherman C, Su D, Weber I, Gadda G. Crystal Structure of Yeast Nitronate Monooxygenase from Cyberlindnera saturnus. Proteins. PMID 29383742 DOI: 10.1002/Prot.25470 |
0.469 |
|
| 2018 |
Romero E, Gómez Castellanos JR, Gadda G, Fraaije MW, Mattevi A. Same Substrate, Many Reactions: Oxygen Activation in Flavoenzymes. Chemical Reviews. PMID 29323892 DOI: 10.1021/Acs.Chemrev.7B00650 |
0.409 |
|
| 2017 |
Su D, Yuan H, Gadda G. A Reversible, Charge-Induced Intramolecular C4a-S-Cysteinyl-Flavin in Choline Oxidase Variant S101C. Biochemistry. 56: 6677-6690. PMID 29190076 DOI: 10.1021/Acs.Biochem.7B00958 |
0.681 |
|
| 2017 |
Gadda G, Yuan H. Substitutions of S101 decrease proton and hydride transfers in the oxidation of betaine aldehyde by choline oxidase. Archives of Biochemistry and Biophysics. 634: 76-82. PMID 29029877 DOI: 10.1016/J.Abb.2017.10.004 |
0.706 |
|
| 2017 |
Sobrado P, Gadda G. Introduction to flavoproteins: Beyond the classical paradigms. Archives of Biochemistry and Biophysics. PMID 28870454 DOI: 10.1016/J.Abb.2017.08.016 |
0.553 |
|
| 2017 |
Uluisik R, Romero E, Gadda G. Evidence for proton tunneling and a transient covalent flavin-substrate adduct in choline oxidase S101A. Biochimica Et Biophysica Acta. PMID 28843728 DOI: 10.1016/J.Bbapap.2017.08.004 |
0.587 |
|
| 2017 |
Robbins JM, Souffrant MG, Hamelberg D, Gadda G, Bommarius AS. Enzyme Mediated Conversion of FAD to 8-formyl FAD in Formate Oxidase Results in Modified Cofactor with Enhanced Catalytic Properties. Biochemistry. PMID 28640638 DOI: 10.1021/Acs.Biochem.7B00335 |
0.582 |
|
| 2017 |
Ouedraogo D, Ball J, Iyer A, Reis RAG, Vodovoz M, Gadda G. Amine oxidation by d-arginine dehydrogenase in Pseudomonas aeruginosa. Archives of Biochemistry and Biophysics. PMID 28625766 DOI: 10.1016/J.Abb.2017.06.013 |
0.529 |
|
| 2017 |
Ouedraogo D, Souffrant M, Vasquez S, Hamelberg D, Gadda G. Importance of Loop L1 Dynamics for Substrate Capture and Catalysis in Pseudomonas aeruginosa D-Arginine Dehydrogenase. Biochemistry. PMID 28445031 DOI: 10.1021/Acs.Biochem.7B00098 |
0.548 |
|
| 2016 |
Ball J, Salvi F, Gadda G. Functional Annotation of a Presumed Nitronate Monooxygenase Reveals a New Class of NADH:quinone Reductases. The Journal of Biological Chemistry. PMID 27502282 DOI: 10.1074/Jbc.M116.739151 |
0.549 |
|
| 2016 |
Sachla AJ, Ouattara M, Romero E, Agniswamy J, Weber IT, Gadda G, Eichenbaum Z. In vitro heme biotransformation by the HupZ enzyme from Group A streptococcus. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. PMID 27154580 DOI: 10.1007/S10534-016-9937-1 |
0.436 |
|
| 2016 |
Salvi F, Rodriguez I, Hamelberg D, Gadda G. Role of F357 as an Oxygen Gate in the Oxidative Half-Reaction of Choline Oxidase. Biochemistry. 55: 1473-84. PMID 26907558 DOI: 10.1021/Acs.Biochem.5B01356 |
0.522 |
|
| 2016 |
Barman A, Smitherman C, Souffrant M, Gadda G, Hamelberg D. Conserved Hydration Sites in Pin1 Reveal a Distinctive Water Recognition Motif in Proteins. Journal of Chemical Information and Modeling. 56: 139-47. PMID 26651388 DOI: 10.1021/Acs.Jcim.5B00560 |
0.301 |
|
| 2016 |
Romero E, Ladani ST, Hamelberg D, Gadda G. Solvent-Slaved Motions in the Hydride Tunneling Reaction Catalyzed by Human Glycolate Oxidase Acs Catalysis. 6: 2113-2120. DOI: 10.1021/Acscatal.5B02889 |
0.477 |
|
| 2015 |
Ball J, Bui QV, Gannavaram S, Gadda G. Importance of glutamate 87 and the substrate α-amine for the reaction catalyzed by D-arginine dehydrogenase. Archives of Biochemistry and Biophysics. 568: 56-63. PMID 25637657 DOI: 10.1016/J.Abb.2015.01.017 |
0.44 |
|
| 2015 |
Smitherman C, Rungsrisuriyachai K, Germann MW, Gadda G. Identification of the catalytic base for alcohol activation in choline oxidase. Biochemistry. 54: 413-21. PMID 25478900 DOI: 10.1021/Bi500982Y |
0.843 |
|
| 2014 |
Romero E, Gadda G. Alcohol oxidation by flavoenzymes. Biomolecular Concepts. 5: 299-318. PMID 25372761 DOI: 10.1515/Bmc-2014-0016 |
0.559 |
|
| 2014 |
Gannavaram S, Sirin S, Sherman W, Gadda G. Mechanistic and computational studies of the reductive half-reaction of tyrosine to phenylalanine active site variants of D-arginine dehydrogenase. Biochemistry. 53: 6574-83. PMID 25243743 DOI: 10.1021/Bi500917Q |
0.592 |
|
| 2014 |
Salvi F, Agniswamy J, Yuan H, Vercammen K, Pelicaen R, Cornelis P, Spain JC, Weber IT, Gadda G. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II. The Journal of Biological Chemistry. 289: 23764-75. PMID 25002579 DOI: 10.1074/Jbc.M114.577791 |
0.694 |
|
| 2014 |
Salvi F, Wang YF, Weber IT, Gadda G. Structure of choline oxidase in complex with the reaction product glycine betaine. Acta Crystallographica. Section D, Biological Crystallography. 70: 405-13. PMID 24531474 DOI: 10.1107/S1399004713029283 |
0.518 |
|
| 2014 |
Gadda G. Cofactor assisted enzymatic catalysis. Archives of Biochemistry and Biophysics. 544: 1. PMID 24491815 DOI: 10.1016/J.Abb.2014.01.012 |
0.473 |
|
| 2013 |
Ouattara M, Pennati A, Devlin DJ, Huang YS, Gadda G, Eichenbaum Z. Kinetics of heme transfer by the Shr NEAT domains of Group A Streptococcus. Archives of Biochemistry and Biophysics. 538: 71-9. PMID 23993953 DOI: 10.1016/J.Abb.2013.08.009 |
0.317 |
|
| 2013 |
Salvi F, Gadda G. Human choline dehydrogenase: medical promises and biochemical challenges. Archives of Biochemistry and Biophysics. 537: 243-52. PMID 23906661 DOI: 10.1016/J.Abb.2013.07.018 |
0.411 |
|
| 2013 |
Francis K, Smitherman C, Nishino SF, Spain JC, Gadda G. The biochemistry of the metabolic poison propionate 3-nitronate and its conjugate acid, 3-nitropropionate. Iubmb Life. 65: 759-68. PMID 23893873 DOI: 10.1002/Iub.1195 |
0.437 |
|
| 2013 |
Gadda G, Fitzpatrick PF. Solvent isotope and viscosity effects on the steady-state kinetics of the flavoprotein nitroalkane oxidase. Febs Letters. 587: 2785-9. PMID 23660407 DOI: 10.1016/J.Febslet.2013.04.021 |
0.582 |
|
| 2013 |
Lambou K, Pennati A, Valsecchi I, Tada R, Sherman S, Sato H, Beau R, Gadda G, Latgé JP. Pathway of glycine betaine biosynthesis in Aspergillus fumigatus. Eukaryotic Cell. 12: 853-63. PMID 23563483 DOI: 10.1128/Ec.00348-12 |
0.376 |
|
| 2013 |
Smitherman C, Gadda G. Evidence for a transient peroxynitro acid in the reaction catalyzed by nitronate monooxygenase with propionate 3-nitronate. Biochemistry. 52: 2694-704. PMID 23530838 DOI: 10.1021/Bi400030D |
0.602 |
|
| 2013 |
Gannavaram S, Gadda G. Relative timing of hydrogen and proton transfers in the reaction of flavin oxidation catalyzed by choline oxidase. Biochemistry. 52: 1221-6. PMID 23339467 DOI: 10.1021/Bi3016235 |
0.484 |
|
| 2012 |
Francis K, Nishino SF, Spain JC, Gadda G. A novel activity for fungal nitronate monooxygenase: detoxification of the metabolic inhibitor propionate-3-nitronate. Archives of Biochemistry and Biophysics. 521: 84-9. PMID 22464989 DOI: 10.1016/J.Abb.2012.03.015 |
0.469 |
|
| 2012 |
Gadda G. Oxygen activation in flavoprotein oxidases: the importance of being positive. Biochemistry. 51: 2662-9. PMID 22432926 DOI: 10.1021/Bi300227D |
0.464 |
|
| 2011 |
Yuan H, Xin Y, Hamelberg D, Gadda G. Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects. Journal of the American Chemical Society. 133: 18957-65. PMID 21999550 DOI: 10.1021/Ja2082729 |
0.745 |
|
| 2011 |
Fu G, Yuan H, Wang S, Gadda G, Weber IT. Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase. Biochemistry. 50: 6292-4. PMID 21707047 DOI: 10.1021/Bi200831A |
0.609 |
|
| 2011 |
Yuan H, Gadda G. Importance of a serine proximal to the C(4a) and N(5) flavin atoms for hydride transfer in choline oxidase. Biochemistry. 50: 770-9. PMID 21174412 DOI: 10.1021/Bi101837U |
0.709 |
|
| 2011 |
Pennati A, Gadda G. Stabilization of an intermediate in the oxidative half-reaction of human liver glycolate oxidase. Biochemistry. 50: 1-3. PMID 21141873 DOI: 10.1021/Bi101387W |
0.527 |
|
| 2010 |
Yuan H, Fu G, Brooks PT, Weber I, Gadda G. Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa. Biochemistry. 49: 9542-50. PMID 20932054 DOI: 10.1021/Bi101420W |
0.706 |
|
| 2010 |
Fu G, Yuan H, Li C, Lu CD, Gadda G, Weber IT. Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase. Biochemistry. 49: 8535-45. PMID 20809650 DOI: 10.1021/Bi1005865 |
0.658 |
|
| 2010 |
Finnegan S, Yuan H, Wang YF, Orville AM, Weber IT, Gadda G. Structural and kinetic studies on the Ser101Ala variant of choline oxidase: catalysis by compromise. Archives of Biochemistry and Biophysics. 501: 207-13. PMID 20561507 DOI: 10.1016/J.Abb.2010.06.014 |
0.787 |
|
| 2010 |
Quaye O, Nguyen T, Gannavaram S, Pennati A, Gadda G. Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue. Archives of Biochemistry and Biophysics. 499: 1-5. PMID 20447376 DOI: 10.1016/J.Abb.2010.04.024 |
0.77 |
|
| 2010 |
Finnegan S, Agniswamy J, Weber IT, Gadda G. Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase. Biochemistry. 49: 2952-61. PMID 20184377 DOI: 10.1021/Bi902048C |
0.741 |
|
| 2010 |
Rungsrisuriyachai K, Gadda G. Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase. Biochemistry. 49: 2483-90. PMID 20163155 DOI: 10.1021/Bi901796A |
0.837 |
|
| 2010 |
Gadda G. Guest editor's introduction. Special issue on oxidative enzymes. Archives of Biochemistry and Biophysics. 493: 1-2. PMID 20103389 DOI: 10.1016/J.Abb.2009.12.009 |
0.475 |
|
| 2010 |
Gadda G, Francis K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Archives of Biochemistry and Biophysics. 493: 53-61. PMID 19577534 DOI: 10.1016/J.Abb.2009.06.018 |
0.558 |
|
| 2009 |
Pennati A, Gadda G. Involvement of ionizable groups in catalysis of human liver glycolate oxidase. The Journal of Biological Chemistry. 284: 31214-22. PMID 19758989 DOI: 10.1074/Jbc.M109.040063 |
0.567 |
|
| 2009 |
Xin Y, Gadda G, Hamelberg D. The cluster of hydrophobic residues controls the entrance to the active site of choline oxidase. Biochemistry. 48: 9599-605. PMID 19728743 DOI: 10.1021/Bi901295A |
0.48 |
|
| 2009 |
Francis K, Gadda G. Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase. Bioorganic Chemistry. 37: 167-72. PMID 19683782 DOI: 10.1016/J.Bioorg.2009.07.005 |
0.553 |
|
| 2009 |
Quaye O, Gadda G. Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase. Archives of Biochemistry and Biophysics. 489: 10-4. PMID 19653994 DOI: 10.1016/J.Abb.2009.07.021 |
0.787 |
|
| 2009 |
Quaye O, Cowins S, Gadda G. Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase. The Journal of Biological Chemistry. 284: 16990-7. PMID 19398559 DOI: 10.1074/Jbc.M109.003715 |
0.749 |
|
| 2009 |
Chen N, Zou J, Wang S, Ye Y, Huang Y, Gadda G, Yang JJ. Designing protease sensors for real-time imaging of trypsin activation in pancreatic cancer cells. Biochemistry. 48: 3519-26. PMID 19271729 DOI: 10.1021/Bi802289V |
0.303 |
|
| 2009 |
Francis K, Gadda G. Inflated kinetic isotope effects in the branched mechanism of Neurospora crassa 2-nitropropane dioxygenase. Biochemistry. 48: 2403-10. PMID 19199786 DOI: 10.1021/Bi802238J |
0.544 |
|
| 2009 |
Rungsrisuriyachai K, Gadda G. A pH switch affects the steady-state kinetic mechanism of pyranose 2-oxidase from Trametes ochracea. Archives of Biochemistry and Biophysics. 483: 10-5. PMID 19146821 DOI: 10.1016/J.Abb.2008.12.018 |
0.827 |
|
| 2009 |
Orville AM, Lountos GT, Finnegan S, Gadda G, Prabhakar R. Crystallographic, spectroscopic, and computational analysis of a flavin C4a-oxygen adduct in choline oxidase. Biochemistry. 48: 720-8. PMID 19133805 DOI: 10.1021/Bi801918U |
0.575 |
|
| 2009 |
Kamio M, Ko KC, Zheng S, Wang B, Collins SL, Gadda G, Tai PC, Derby CD. The chemistry of escapin: identification and quantification of the components in the complex mixture generated by an L-amino acid oxidase in the defensive secretion of the sea snail Aplysia californica. Chemistry (Weinheim An Der Bergstrasse, Germany). 15: 1597-603. PMID 19130530 DOI: 10.1002/Chem.200801696 |
0.345 |
|
| 2009 |
Kamio M, Ko K, Zheng S, Wang B, Collins S, Gadda G, Tai P, Derby C. Cover Picture: The Chemistry of Escapin: Identification and Quantification of the Components in the Complex Mixture Generated by an L-Amino Acid Oxidase in the Defensive Secretion of the Sea SnailAplysia californica(Chem. Eur. J. 7/2009) Chemistry - a European Journal. 15: 1535-1535. DOI: 10.1002/Chem.200990013 |
0.355 |
|
| 2008 |
Finnegan S, Gadda G. Substitution of an active site valine uncovers a kinetically slow equilibrium between competent and incompetent forms of choline oxidase. Biochemistry. 47: 13850-61. PMID 19053262 DOI: 10.1021/Bi801424P |
0.753 |
|
| 2008 |
Gadda G. Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases. Biochemistry. 47: 13745-53. PMID 19053234 DOI: 10.1021/Bi801994C |
0.556 |
|
| 2008 |
Francis K, Gadda G. The nonoxidative conversion of nitroethane to ethylnitronate in Neurospora crassa 2-nitropropane dioxygenase is catalyzed by histidine 196. Biochemistry. 47: 9136-44. PMID 18690716 DOI: 10.1021/Bi801013E |
0.587 |
|
| 2008 |
Rungsrisuriyachai K, Gadda G. On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase. Biochemistry. 47: 6762-9. PMID 18540638 DOI: 10.1021/Bi800650W |
0.847 |
|
| 2008 |
Mijatovic S, Gadda G. Oxidation of alkyl nitronates catalyzed by 2-nitropropane dioxygenase from Hansenula mrakii. Archives of Biochemistry and Biophysics. 473: 61-8. PMID 18329375 DOI: 10.1016/J.Abb.2008.02.029 |
0.602 |
|
| 2008 |
Pennati A, Zanetti G, Aliverti A, Gadda G. Effect of salt and pH on the reductive half-reaction of Mycobacterium tuberculosis FprA with NADPH. Biochemistry. 47: 3418-25. PMID 18293930 DOI: 10.1021/Bi702250H |
0.496 |
|
| 2008 |
Quaye O, Lountos GT, Fan F, Orville AM, Gadda G. Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase. Biochemistry. 47: 243-56. PMID 18072756 DOI: 10.1021/Bi7017943 |
0.808 |
|
| 2007 |
Fan F, Gadda G. An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase. Biochemistry. 46: 6402-8. PMID 17472346 DOI: 10.1021/Bi700255V |
0.662 |
|
| 2007 |
Zargari A, Selander C, Rasool O, Ghanem M, Gadda G, Crameri R, Scheynius A. Mala s 12 is a major allergen in patients with atopic eczema and has sequence similarities to the GMC oxidoreductase family. Allergy. 62: 695-703. PMID 17313403 DOI: 10.1111/J.1398-9995.2006.01291.X |
0.595 |
|
| 2007 |
Hoang JV, Gadda G. Trapping choline oxidase in a nonfunctional conformation by freezing at low pH. Proteins. 66: 611-20. PMID 17143885 DOI: 10.1002/Prot.21238 |
0.558 |
|
| 2007 |
Gadda G, Francis K, Belaineh M. The Mechanism of 2‐Nitropropane Dioxygenase: a Model for Flavin Semiquinone Intermediates in Enzymatic Catalysis The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A272 |
0.482 |
|
| 2006 |
Francis K, Gadda G. Probing the chemical steps of nitroalkane oxidation catalyzed by 2-nitropropane dioxygenase with solvent viscosity, pH, and substrate kinetic isotope effects. Biochemistry. 45: 13889-98. PMID 17105207 DOI: 10.1021/Bi060566L |
0.598 |
|
| 2006 |
Gadda G, Fan F, Hoang JV. On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase. Archives of Biochemistry and Biophysics. 451: 182-7. PMID 16713988 DOI: 10.1016/J.Abb.2006.04.005 |
0.658 |
|
| 2006 |
Ghanem M, Gadda G. Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase. Biochemistry. 45: 3437-47. PMID 16519539 DOI: 10.1021/Bi052514M |
0.673 |
|
| 2006 |
Fan F, Germann MW, Gadda G. Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde. Biochemistry. 45: 1979-86. PMID 16460045 DOI: 10.1021/Bi0517537 |
0.693 |
|
| 2005 |
Fan F, Gadda G. Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: correlating reversible hydride transfer with environmentally enhanced tunneling. Journal of the American Chemical Society. 127: 17954-61. PMID 16351127 DOI: 10.1021/Ja0560377 |
0.618 |
|
| 2005 |
Fan F, Gadda G. On the catalytic mechanism of choline oxidase. Journal of the American Chemical Society. 127: 2067-74. PMID 15713082 DOI: 10.1021/Ja044541Q |
0.619 |
|
| 2005 |
Ghanem M, Gadda G. On the catalytic role of the conserved active site residue His466 of choline oxidase. Biochemistry. 44: 893-904. PMID 15654745 DOI: 10.1021/Bi048056J |
0.771 |
|
| 2005 |
Francis K, Russell B, Gadda G. Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase. The Journal of Biological Chemistry. 280: 5195-204. PMID 15582992 DOI: 10.1074/Jbc.M411249200 |
0.623 |
|
| 2004 |
Gadda G, Powell NL, Menon P. The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase. Archives of Biochemistry and Biophysics. 430: 264-73. PMID 15369826 DOI: 10.1016/J.Abb.2004.07.011 |
0.812 |
|
| 2004 |
Fan F, Ghanem M, Gadda G. Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance. Archives of Biochemistry and Biophysics. 421: 149-58. PMID 14678796 DOI: 10.1016/J.Abb.2003.10.003 |
0.71 |
|
| 2003 |
Ghanem M, Fan F, Francis K, Gadda G. Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis. Biochemistry. 42: 15179-88. PMID 14690428 DOI: 10.1021/Bi035435O |
0.766 |
|
| 2003 |
Gadda G. pH and deuterium kinetic isotope effects studies on the oxidation of choline to betaine-aldehyde catalyzed by choline oxidase. Biochimica Et Biophysica Acta. 1650: 4-9. PMID 12922164 DOI: 10.1016/S1570-9639(03)00188-2 |
0.518 |
|
| 2003 |
Gadda G, McAllister-Wilkins EE. Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata. Applied and Environmental Microbiology. 69: 2126-32. PMID 12676692 DOI: 10.1128/Aem.69.4.2126-2132.2003 |
0.543 |
|
| 2003 |
Gadda G. Kinetic mechanism of choline oxidase from Arthrobacter globiformis. Biochimica Et Biophysica Acta. 1646: 112-8. PMID 12637017 DOI: 10.1016/S1570-9639(03)00003-7 |
0.604 |
|
| 2002 |
Daubner SC, Gadda G, Valley MP, Fitzpatrick PF. Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily. Proceedings of the National Academy of Sciences of the United States of America. 99: 2702-7. PMID 11867731 DOI: 10.1073/Pnas.052527799 |
0.646 |
|
| 2001 |
Gadda G, Banerjee A, Fleming GS, Fitzpatrick PF. Evidence for an essential arginine in the flavoprotein nitroalkane oxidase. Journal of Enzyme Inhibition. 16: 157-63. PMID 11342284 DOI: 10.1080/14756360109162365 |
0.747 |
|
| 2000 |
Gadda G, Choe DY, Fitzpatrick PF. Use of pH and kinetic isotope effects to dissect the effects of substrate size on binding and catalysis by nitroalkane oxidase. Archives of Biochemistry and Biophysics. 382: 138-44. PMID 11051107 DOI: 10.1006/Abbi.2000.2009 |
0.646 |
|
| 2000 |
Gadda G, Banerjee A, Dangott LJ, Fitzpatrick PF. Identification of a cysteine residue in the active site of nitroalkane oxidase by modification with N-ethylmaleimide. The Journal of Biological Chemistry. 275: 31891-5. PMID 10913134 DOI: 10.1074/Jbc.M003679200 |
0.689 |
|
| 2000 |
Gadda G, Fitzpatrick PF. Mechanism of nitroalkane oxidase: 2. pH and kinetic isotope effects. Biochemistry. 39: 1406-10. PMID 10684621 DOI: 10.1021/Bi992255Z |
0.631 |
|
| 2000 |
Gadda G, Fitzpatrick PF. Iso-mechanism of nitroalkane oxidase: 1. Inhibition studies and activation by imidazole. Biochemistry. 39: 1400-5. PMID 10684620 DOI: 10.1021/Bi9922547 |
0.717 |
|
| 2000 |
Gadda G, Banerjee A, Fitzpatrick PF. Identification of an essential tyrosine residue in nitroalkane oxidase by modification with tetranitromethane. Biochemistry. 39: 1162-8. PMID 10653664 DOI: 10.1021/Bi9921743 |
0.708 |
|
| 1999 |
Pollegioni L, Gadda G, Ambrosius D, Ghisla S, Pilone MS. Cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum: Effect of surfactants and organic solvents on activity Biotechnology and Applied Biochemistry. 30: 27-33. PMID 10467115 DOI: 10.1111/J.1470-8744.1999.Tb01155.X |
0.427 |
|
| 1999 |
Gadda G, Dangott LJ, Johnson WH, Whitman CP, Fitzpatrick PF. Characterization of 2-oxo-3-pentynoate as an active-site-directed inactivator of flavoprotein oxidases: identification of active-site peptides in tryptophan 2-monooxygenase. Biochemistry. 38: 5822-8. PMID 10231533 DOI: 10.1021/Bi982777Z |
0.659 |
|
| 1999 |
Gadda G, Fitzpatrick PF. Substrate specificity of a nitroalkane-oxidizing enzyme. Archives of Biochemistry and Biophysics. 363: 309-13. PMID 10068453 DOI: 10.1006/Abbi.1998.1081 |
0.699 |
|
| 1998 |
Gadda G, Fitzpatrick PF. Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum. Biochemistry. 37: 6154-64. PMID 9558355 DOI: 10.1021/Bi973085Y |
0.72 |
|
| 1997 |
Gadda G, Wels G, Pollegioni L, Zucchelli S, Ambrosius D, Pilone MS, Ghisla S. Characterization of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum European Journal of Biochemistry. 250: 369-376. PMID 9428686 DOI: 10.1111/J.1432-1033.1997.0369A.X |
0.598 |
|
| 1997 |
Gadda G, Edmondson RD, Russell DH, Fitzpatrick PF. Identification of the naturally occurring flavin of nitroalkane oxidase from fusarium oxysporum as a 5-nitrobutyl-FAD and conversion of the enzyme to the active FAD-containing form. The Journal of Biological Chemistry. 272: 5563-70. PMID 9038163 DOI: 10.1074/Jbc.272.9.5563 |
0.697 |
|
| 1997 |
Edmondson RD, Gadda G, Fitzpatrick PF, Russell DH. Identification of Native Flavin Adducts Fusarium oxysporum Using Accurate Mass Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry Analytical Chemistry. 69: 2862-2865. DOI: 10.1021/Ac9700989 |
0.484 |
|
| 1995 |
Gadda G, Beretta GL, Pilone MS. Reactivity of histidyl residues in d-amino acid oxidase from Rhodotorula gracilis Febs Letters. 363: 307-310. PMID 7737423 DOI: 10.1016/0014-5793(95)00337-9 |
0.517 |
|
| 1994 |
Gadda G, Negri A, Pilone MS. Reaction of phenylglyoxal with arginine groups in D-amino-acid oxidase from Rhodotorula gracilis Journal of Biological Chemistry. 269: 17809-17814. PMID 7913089 |
0.365 |
|
| 1991 |
Aliverti A, Gadda G, Ronchi S, Zanetti G. Identification of Lys116 as the target of N-ethylmaleimide inactivation of ferredoxin:NADP+ oxidoreductase European Journal of Biochemistry. 198: 21-24. PMID 1904024 DOI: 10.1111/J.1432-1033.1991.Tb15981.X |
0.502 |
|
| 1990 |
Gadda G, Aliverti A, Ronchi S, Zanetti G. Structure-function relationship in spinach ferredoxin-NADP+ reductase as studied by limited proteolysis Journal of Biological Chemistry. 265: 11955-11959. PMID 2195029 |
0.301 |
|
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