Role of multiple binding sites in the inhibition of NADH oxidase by piericidin and rotenone

M. Gutman*, Thomas P. Singer, John E. Casida

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Scatchard plots indicate that 14C-piericidin A and -rotenone bind at 2 specific sites per mole of NADH dehydrogenase in ETP, but the titer found for complex I or mersalyl-treated ETP more closely approximates 1. The curves for inhibition of NADH oxidase by piericidin and rotenone are sigmoidal; this results from an unequal contribution of the 2 specific sites to the inhibition. An unspecific binding site also contributes to the inhibition in a manner reversed by washing the particles with bovine serum albumin (BSA). In contrast, inhibition of NADH-CoQ reductase activity is due entirely to binding at specific site(s) because BSA does not restore activity.

Original languageEnglish
Pages (from-to)615-622
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume37
Issue number4
DOIs
StatePublished - 6 Nov 1969
Externally publishedYes

Funding

FundersFunder number
National Science FoundationGB 82481
National Science Foundation
American Cancer SocietyP 5311
American Cancer Society
American Heart Association67 7061
American Heart Association
U.S. Public Health ServiceHE 10027, ESGM 00049
U.S. Public Health Service
Atomic Energy Commission of Syria113, AT(ll-11-34
Atomic Energy Commission of Syria

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