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Kinetic characteristics of quinone interaction with the photosynthetic reaction center in chromatophore membranes of nonsulfur purple bacteria



Kinetic characteristics of quinone interaction with the photosynthetic reaction center in chromatophore membranes of nonsulfur purple bacteria



Biologicheskie Membrany 2(6): 575-587



Flash-induced redox changes of secondary quinone acceptor (QB) and bacteriochlorophyll dimer P870 of photosynthetic reaction centre have been studied to estimate rate constants of membrane quinone pool and QB exchange in Rhodospirillum rubrum chromatophores. It was shown that slow component of P870 dark reduction after flash excitation and flash-induced QB- binary oscillations both depend on quinone concentration remaining in the membrane after partial extraction by isooctane. The kinetic analysis demonstrated that pseudomonomolecular rate constants of QB binding and unbinding with B site on the photosynthetic reaction centre protein in R. rubrum chromatophores are 4.3 .cntdot. 102 s-1 and 1.3 .cntdot. 102 s-1, resp. The dependence was studied of slow component of dark reduction of flash-oxidized P870 on o-phenantroline concentration, which is known to reversibly substitute QB on its specific binding site; the data allowed to calculate rate constants of o-phenantroline interaction with the reaction centre. The results obtained strongly support the concept that neutral quinone forms (QB, QBH2) function as a quinone pool, connecting a great number of enzymes which are capable to reduce Q to QH2 (reaction centres, succinate dehydrogenase, etc.), with QH2: cytochrome c2-oxidoreductase. In contrast to QB or QBH2, the changed anion-radical quinone form QB. is fixed in the reaction centre of protein structure, probably by means of electrostatic interaction, and can be considered as a kind of prosthetic group.

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