A novel strong competitive inhibitor of complex I

Alexander Kotlyar*, Joel S. Karliner, Gary Cecchini

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


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.

Original languageEnglish
Pages (from-to)4861-4866
Number of pages6
JournalFEBS Letters
Issue number21
StatePublished - 29 Aug 2005


FundersFunder number
U.S. Department of Veterans Affairs
Sandler Foundation


    • Competitive inhibition
    • Complex I
    • Enzyme kinetics
    • NADH-ubiquinone oxidoreductase


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