Genetic evidence for the existence of two quinone related inhibitor binding sites in NADH-CoQ reductase

Biochim Biophys Acta. 1997 Mar 28;1319(1):1-4. doi: 10.1016/s0005-2728(97)00009-1.

Abstract

Using the NADH-CoQ reductase of Rhodobacter capsulatus as a model for the mitochondrial Complex I, we have for the first time isolated bacterial mutants resistant to piericidin-A, a classical inhibitor of the mitochondrial enzyme. Their sensitivity to other inhibitors directed towards the quinone binding domain of complex I gives direct genetic evidence for the existence of two inhibitor binding sites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Electron Transport Complex I
  • Enzyme Inhibitors / pharmacology
  • Furans / pharmacology
  • Multienzyme Complexes / metabolism
  • NADH, NADPH Oxidoreductases / antagonists & inhibitors
  • NADH, NADPH Oxidoreductases / chemistry*
  • NADH, NADPH Oxidoreductases / genetics
  • NADH, NADPH Oxidoreductases / metabolism
  • Pyridines / pharmacology
  • Rhodobacter capsulatus
  • Rotenone / pharmacology

Substances

  • Enzyme Inhibitors
  • Furans
  • Multienzyme Complexes
  • Pyridines
  • Rotenone
  • bullatacin
  • piericidin A
  • NADH oxidase
  • NADH, NADPH Oxidoreductases
  • Electron Transport Complex I