Kinetics and energetics of redox regulation of ATP synthase from chloroplasts.
The rate of ATP hydrolysis catalyzed by the membrane-bound CF0F1 ATP synthase from chloroplasts served as a probe for the determination of the reduction grade of the enzyme treated with dithiothreitol (DTT) or thioredoxin. Rate constants for reduction were obtained. It turns out that reduction by thioredoxin is about a factor of 6,000 more effective than DTT reduction. The activation profiles with respect to delta pH were obtained for reduced and oxidized ATPases. The activation curve of reduced enzyme turns out to have its half-maximum degree of activation at delta pH = 1.65, which is considerably lower than reported hitherto. The corresponding value of the oxidized enzyme has been obtained from the rate of ATP hydrolysis in the case of incomplete reduced ATPases, taking into account the aforementioned rate constants, and comes to delta pH = 3.35.
Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität Berlin, Germany.
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F
Strelow
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Rumberg
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002736:Chloroplasts / Q000201:enzymology*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010084:Oxidation-Reduction; D010944:Plants; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013816:Thermodynamics
D013438:Sulfhydryl Compounds; D000251:Adenosine Triphosphatases