Co-Authors:
Shahak, Y., Institute of Horticulture, The Volcani Center, ARO, Bet-Dagan, Israel
Klughammer, C., Julius-von-Sachs-Institut für Biowissenschaften mit Botanischem Garten, Universität Würzburg, Germany
Schreiber, U., Julius-von-Sachs-Institut für Biowissenschaften mit Botanischem Garten, Universität Würzburg, Germany
Padan, E., Division of Microbial and Molecular Ecology, Institute of Life Sciences, The Hebrew University of Jerusalem, Israel
Herrman, I., Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, Germany
Hauska, G., Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, Germany
Abstract:
The reduction by sulfide of exogenous ubiquinone is compared to the reduction of cytochromes in chromatophores of Rhodobacter capsulatus. From titrations with sulfide values for Vmax of 300 and 10 μmoles reduced/mg bacteriochlorophyll a·h, and for Km of 5 and 3 μM were estimated, for decyl-ubiquinone-and cytochrome c-reduction, respectively. Both reactions are sensitive to KCN, as has been found for sulfide-quinone reductase (SQR) in Oscillatoria limnetica, which is a flavoprotein. Effects of inhibitors interfering with quinone binding sites suggest that at least part of the electron transport from sulfide in R. capsulatus employs the cytochrome bc1-complex via the ubiquinone pool. © 1994 Kluwer Academic Publishers.
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