title: Oxidative phosphorylation and respiratory control phenomenon in Paracoccus denitrificans plasma membrane.
abstract: Changes in respiratory activity, transmembrane electric potential, and ATP synthesis as induced by additions of limited amounts of ADP and P(i) to tightly coupled inverted (inside-out) Paracoccus denitrificans plasma membrane vesicles were traced. The pattern of the changes was qualitatively the same as those observed for coupled mitochondria during the classical State 4-State 3-State 4 transition. Bacterial vesicles devoid of energy-dependent permeability barriers for the substrates of oxidation and phosphorylation were used as a simple experimental model to investigate two possible mechanisms of respiratory control: (i) in State 4 phosphoryl transfer potential (ATP/ADP × P(i)) is equilibrated with proton-motive force by reversibly operating F(1)·F(o)-ATPase (thermodynamic control); (ii) in State 4 apparent "equilibrium" is reached by unidirectional operation of proton motive force-activated F(1)·F(o)-ATP synthase. The data support the kinetic mechanism of the respiratory control phenomenon.
authors.affiliation: Department of Biochemistry, Faculty of Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
authors.forename: T V
authors.initials: TV
authors.lastname: Zharova
authors.forename: A D
authors.initials: AD
authors.lastname: Vinogradov
mesh_terms: D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000818:Animals; D055162:Biocatalysis; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism*; D004579:Electron Transport; D007700:Kinetics; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism; D010084:Oxidation-Reduction; D010085:Oxidative Phosphorylation; D010231:Paracoccus denitrificans / Q000166:cytology* / Q000378:metabolism*; D051381:Rats
chemical_list: D000255:Adenosine Triphosphate; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases