期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1837, 期 10, 页码 1801-1809出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2014.05.357
关键词
Enzyme kinetics; Nitrate reductase; Electrochemistry; EPR spectroscopy
资金
- CNRS
- CEA
- Aix-Marseille Universite
- Agence Nationale de la Recherche (ANR MC2) [11-BSV5-005-01]
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. (C) 2014 Elsevier B.V. All rights reserved.
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