The reaction sites of rotenone and ubiquinone with mitochondrial NADH dehydrogenase

Thomas P. Singer*, Rona R. Ramsay

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

70 Citations (Scopus)

Abstract

This article summarizes recent studies in the authors' and other laboratories of selective inhibitors acting at the 'rotenone' site and at the Q binding site in the NADH-Q oxidoreductase segment of the respiratory chain. A wide array of inhibitors act at the rotenone site to block electron flux from the enzyme to the Q pool. Using evidence from studies with rotenone, piericidin A, and analogs of the neurotoxic N-methyl-4-phenylpyridinium, we have proposed two binding sites for these inhibitors, both of which must be occupied for complete inhibition of NADH oxidation.

Original languageEnglish
Pages (from-to)198-202
Number of pages5
JournalBBA - Bioenergetics
Volume1187
Issue number2
DOIs
Publication statusPublished - 30 Aug 1994

Keywords

  • Complex I
  • MPP
  • NADH dehydrogenase
  • NADH-Q oxidoreductase
  • Piericidin A
  • Q
  • Rotenone
  • Ubiquinone

Fingerprint

Dive into the research topics of 'The reaction sites of rotenone and ubiquinone with mitochondrial NADH dehydrogenase'. Together they form a unique fingerprint.

Cite this