Partial reversion of the electrogenic reaction in the ubiquinol: cytochrome c2-oxidoreductase of Rhodobacter sphaeroides chromatophores under neutral and alkaline conditions. 1990

Mulkidjanian AYa, and M D Mamedov, and Semenov AYu, and V P Shinkarev, and M I Verkhovsky, and L A Drachev
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Department of Biology, Moscow State University, USSR.

The interaction of the photosynthetic reaction center (RC)-generated ubiquinol with the ubiquinone-reducing center C of ubiquinol:cytochrome c2-oxidoreductase (bc1-complex) has been studied electrometrically in Rhodobacter sphaeroides chromatophores. The addition of myxothiazol inhibited the ubiquinol-oxidizing center Z, suppressing the phases of membrane potential generation by the bc1-complex, but at the same time induced an electrogenic phase of opposite polarity, sensitive to antimycin A, the inhibitor of center C. The rise time of this reverse phase varied from 3 ms at pH 6.0 to 1 ms at pH 9.5. At pH greater than 9.5 the reverse phase was limited by the rate of ubiquinol formation in RC. The magnitude of the reverse phase was constant within the pH range 7.5-10.0. It is assumed that the reverse phase is due to the electrogenic deprotonation reaction which takes place after the binding of the RC-generated ubiquinol to center C.

UI MeSH Term Description Entries
D008564 Membrane Potentials The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization). Resting Potentials,Transmembrane Potentials,Delta Psi,Resting Membrane Potential,Transmembrane Electrical Potential Difference,Transmembrane Potential Difference,Difference, Transmembrane Potential,Differences, Transmembrane Potential,Membrane Potential,Membrane Potential, Resting,Membrane Potentials, Resting,Potential Difference, Transmembrane,Potential Differences, Transmembrane,Potential, Membrane,Potential, Resting,Potential, Transmembrane,Potentials, Membrane,Potentials, Resting,Potentials, Transmembrane,Resting Membrane Potentials,Resting Potential,Transmembrane Potential,Transmembrane Potential Differences
D008689 Methacrylates Acrylic acids or acrylates which are substituted in the C-2 position with a methyl group. Methacrylate
D010788 Photosynthesis The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001) Calvin Cycle,Calvin-Benson Cycle,Calvin-Benson-Bassham Cycle,Carbon Fixation, Photosynthetic,Reductive Pentose Phosphate Cycle,Dark Reactions of Photosynthesis,Calvin Benson Bassham Cycle,Calvin Benson Cycle,Cycle, Calvin,Cycle, Calvin-Benson,Cycle, Calvin-Benson-Bassham,Photosynthesis Dark Reaction,Photosynthesis Dark Reactions,Photosynthetic Carbon Fixation
D003574 Cytochrome c Group A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539) Cytochromes Type c,Group, Cytochrome c,Type c, Cytochromes
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D012242 Rhodobacter sphaeroides Spherical phototrophic bacteria found in mud and stagnant water exposed to light. Rhodopseudomonas sphaeroides,Rhodobacter spheroides,Rhodopseudomonas spheroides
D013844 Thiazoles Heterocyclic compounds where the ring system is composed of three CARBON atoms, a SULFUR and NITROGEN atoms. Thiazole
D014450 Electron Transport Complex III A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane. Complex III,Cytochrome bc1 Complex,Ubiquinol-Cytochrome-c Reductase,Coenzyme Q-Cytochrome-c Reductase,Coenzyme QH2-Cytochrome-c Reductase,Core I Protein, UCCreductase,Core I Protein, Ubiquinol-Cytochrome c Reductase,Core II Protein, UCCreductase,Core II Protein, Ubiquinol-Cytochrome c Reductase,Cytochrome b-c2 Oxidoreductase,Cytochrome bc1,Dihydroubiquinone-Cytochrome-c Reductase,QH(2)-Cytochrome-c Reductase,QH(2)-Ferricytochrome-c Oxidoreductase,Ubihydroquinone-Cytochrome-c Reductase,Ubiquinol-Cytochrome c Reductase,Ubiquinone-Cytochrome b-c2 Oxidoreductase,Coenzyme Q Cytochrome c Reductase,Coenzyme QH2 Cytochrome c Reductase,Core I Protein, Ubiquinol Cytochrome c Reductase,Core II Protein, Ubiquinol Cytochrome c Reductase,Cytochrome b c2 Oxidoreductase,Dihydroubiquinone Cytochrome c Reductase,Reductase, Ubiquinol-Cytochrome c,Ubihydroquinone Cytochrome c Reductase,Ubiquinol Cytochrome c Reductase,Ubiquinone Cytochrome b c2 Oxidoreductase
D014451 Ubiquinone A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals. Coenzyme Q
D045322 Photosynthetic Reaction Center Complex Proteins Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II. Photosynthetic Complex,Photosynthetic Reaction Center,Photosynthetic Reaction Center Complex Protein,Photosynthetic Complexes,Photosynthetic Reaction Centers,Center, Photosynthetic Reaction,Complex, Photosynthetic,Complexes, Photosynthetic,Reaction Center, Photosynthetic,Reaction Centers, Photosynthetic

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