@article{1c53947115a4472db34ef96db170bfbc,
title = "A novel strong competitive inhibitor of complex I",
abstract = "Alkaline incubation of NADH results in the formation of a very potent inhibitor of complex I (NADH:ubiquinone oxidoreductase). Mass spectroscopy (molecular mass equal to 696) and absorption spectroscopy suggest that the inhibitor is derived from attachment of two oxygen atoms to the nicotinamide moiety of NADH. The inhibitor is competitive with respect to NADH with a K i of about 10-8 M. The inhibitor efficiently suppresses NADH-oxidase, NADH-artificial acceptor reductase, and NADH-quinone reductase reactions catalyzed by submitochondrial particles, as well as the reactions catalyzed by either isolated complex I or the three subunit flavoprotein fragment of complex I.",
keywords = "Competitive inhibition, Complex I, Enzyme kinetics, NADH-ubiquinone oxidoreductase",
author = "Alexander Kotlyar and Karliner, {Joel S.} and Gary Cecchini",
note = "Funding Information: The authors are thankful to Dr. Menahem Gutman, Elena Maklashina, and Andrei Vinogradov for very useful suggestions, Dr. Y. Hatefi for his generous gift of FP and complex I, and Dr. Stephen Massa for help with the ChemNavigator and SciFinder searches. We are also very grateful to Michael K. Johnson and Elizabeth Walterst for EPR analysis of the interaction of the inhibitor with complex I. This study was supported by the Department of Veterans Affairs and the Sandler Research Foundation.",
year = "2005",
month = aug,
day = "29",
doi = "10.1016/j.febslet.2005.07.076",
language = "אנגלית",
volume = "579",
pages = "4861--4866",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley-Blackwell",
number = "21",
}