ascorbic-acid and 2-3-dimethoxy-5-methyl-6-decyl-1-4-benzoquinone

ascorbic-acid has been researched along with 2-3-dimethoxy-5-methyl-6-decyl-1-4-benzoquinone* in 1 studies

Other Studies

1 other study(ies) available for ascorbic-acid and 2-3-dimethoxy-5-methyl-6-decyl-1-4-benzoquinone

Article	Year
Evidence for a two proton dependent redox equilibrium in an archaeal Rieske iron-sulfur cluster. Biochemical and biophysical research communications, 1994, Jul-15, Volume: 202, Issue:1 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. Topics: Animals; Ascorbic Acid; Cell Membrane; Cytochrome c Group; Electron Transport Complex III; Horses; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Kinetics; Membrane Proteins; Myocardium; Oxidation-Reduction; Sulfolobus acidocaldarius; Ubiquinone	1994

Article

Year

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

Biochemical and biophysical research communications, 1994, Jul-15, Volume: 202, Issue:1

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.

Topics: Animals; Ascorbic Acid; Cell Membrane; Cytochrome c Group; Electron Transport Complex III; Horses; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Kinetics; Membrane Proteins; Myocardium; Oxidation-Reduction; Sulfolobus acidocaldarius; Ubiquinone

1994