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Volume 272, Number 27, Issue of July 4, 1997 pp. 16924-16927
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Kinetics and Thioredoxin Specificity of Thiol Modulation of the Chloroplast H⁺-ATPase

(Received for publication, February 4, 1997, and in revised form, March 25, 1997)

Oliver Schwarz , Peter Schürmann ^§ and Heinrich Strotmann

From the  Institut für Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, D-40225 Düsseldorf, Federal Republic of Germany and ^§ Laboratoire de Biochimie végétale, Université de Neuchâtel, CH-2007 Neuchâtel, Switzerland

The kinetics of thiol modulation of the chloroplast H⁺-ATPase (CF₀CF₁) in membrana were analyzed by employing thioredoxins that were kept reduced by 0.1 mM dithiothreitol. The kinetics of thiol modulation depend on the extent of the proton gradient. The process is an exponential function of the thioredoxin concentration and reaction time and can be described by an irreversible second order reaction. The results indicate that the formation of the complex between thioredoxin and CF₀CF₁ is slow compared with the subsequent reduction step. Furthermore we have compared the efficiencies of the Escherichia coli thioredoxin Trx and the two chloroplast thioredoxins Tr-m and Tr-f. The second order rate constants are 0.057 (Tr-f), 0.024 (Trx), and 0.010 s¹ µM¹ (Tr-m) suggesting that Tr-f rather than Tr-m is the physiological reductant for the chloroplast ATPase. The often employed artificial reductant dithiothreitol exhibits a second order rate constant in thiol modulation of 1.02·10⁶ s¹ µM¹.

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