Evidence for a two proton dependent redox equilibrium in an archaeal Rieske iron-sulfur cluster

Biochem Biophys Res Commun. 1994 Jul 15;202(1):252-7. doi: 10.1006/bbrc.1994.1920.

Abstract

The recently detected Rieske iron-sulfur center in the membrane of the thermoacidophilic archaeon Sulfolobus acidocaldarius (Anemüller et al., 1993, FEBS Lett. 318, 61-64) was further characterized by EPR spectroscopy, coupled to redox-potentiometry and functional studies. The reduction potential is pH-dependent above pH 6, revealing the influence of two ionization equilibria in the oxidized form, with pKaox-values of 6.2 and 8.5. Above pH 9, the slope of the curve is--120 mV/pH-unit. A partially purified fraction exerted a ubiquinol-cytochrome c oxidoreductase activity. To our knowledge, for the first time, in a membrane bound Rieske iron-sulfur protein, unequivocal evidence for a two proton dependent redox equilibrium is presented.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Ascorbic Acid / pharmacology
  • Cell Membrane / metabolism
  • Cytochrome c Group / metabolism
  • Electron Transport Complex III*
  • Horses
  • Hydrogen-Ion Concentration
  • Iron-Sulfur Proteins / isolation & purification
  • Iron-Sulfur Proteins / metabolism*
  • Kinetics
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism
  • Myocardium / metabolism
  • Oxidation-Reduction
  • Sulfolobus acidocaldarius / metabolism*
  • Ubiquinone / analogs & derivatives
  • Ubiquinone / pharmacology

Substances

  • Cytochrome c Group
  • Iron-Sulfur Proteins
  • Membrane Proteins
  • Rieske iron-sulfur protein
  • Ubiquinone
  • 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
  • Electron Transport Complex III
  • Ascorbic Acid