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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sabaty, Monique Arnoux, Pascal Burlat, Bénédicte Pignol, David Léger, Christophe Jacques, Julien G. J. Guigliarelli, Bruno Fourmond, Vincent |
| Description | Author Affiliation: Jacques JG ( Aix-Marseille Université, CNRS, BIP UMR 7281, 31 Chemin J. Aiguier, F-13402 Marseille Cedex 20, France.); Burlat B ( Aix-Marseille Université, CNRS, BIP UMR 7281, 31 Chemin J. Aiguier, F-13402 Marseille Cedex 20, France.); Arnoux P ( Aix-Marseille Université, CNRS, CEA, DSV/IBEB/LBC UMR 7265, F-13108 Saint Paul Lez Durance, France.); Sabaty M ( Aix-Marseille Université, CNRS, CEA, DSV/IBEB/LBC UMR 7265, F-13108 Saint Paul Lez Durance, France.); Guigliarelli B ( Aix-Marseille Université, CNRS, BIP UMR 7281, 31 Chemin J. Aiguier, F-13402 Marseille Cedex 20, France.); Léger C ( Aix-Marseille Université, CNRS, BIP UMR 7281, 31 Chemin J. Aiguier, F-13402 Marseille Cedex 20, France.); Pignol D ( Aix-Marseille Université, CNRS, CEA, DSV/IBEB/LBC UMR 7265, F-13108 Saint Paul Lez Durance, France.); Fourmond V ( Aix-Marseille Université, CNRS, BIP UMR 7281, 31 Chemin J. Aiguier, F-13402 Marseille Cedex 20, France. Electronic address: vincent.fourmond@imm.cnrs.fr.) |
| Abstract | Periplasmic nitrate reductase catalyzes the reduction of nitrate into nitrite using a mononuclear molybdenum cofactor that has nearly the same structure in all enzymes of the DMSO reductase family. In previous electrochemical investigations, we found that the enzyme exists in several inactive states, some of which may have been previously isolated and mistaken for catalytic intermediates. In particular, the enzyme slowly and reversibly inactivates when exposed to high concentrations of nitrate. Here, we study the kinetics of substrate inhibition and its dependence on electrode potential and substrate concentration to learn about the properties of the active and inactive forms of the enzyme. We conclude that the substrate-inhibited enzyme never significantly accumulates in the EPR-active Mo(+ V) state. This conclusion is relevant to spectroscopic investigations where attempts are made to trap a Mo(+ V) catalytic intermediate using high concentrations of nitrate. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 10 |
| Volume Number | 1837 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-10-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Nitrate Reductase Antagonists & Inhibitors Periplasm Enzymology Kinetics Nitrites Metabolism Oxidation-Reduction Substrate Specificity Thermodynamics Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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