Abstract
Chromatophores from Rhodopseudomonas capsulata grown photoheterotrophically with malate as both reductant and carbon source contain at least six iron sulphur centres. These are a High Potential Iron Sulphur Protein (HiPIP, probably centre S-3 of the succinic-dehydrogenase), a Rieske centre (centered at g=1.90) and four ferredoxins centered at g=1.94. Previous studies on mutants (Zannoni and Ingledew (1983) FEMS Lett 17, 331–334) have shown that two of these ferredoxins may be assigned to the NADH-dehydrogenase and two to the succinic-dehydrogenase. In this paper we report a complete analysis of the wild-type strain and attempt a functional characterization of the iron sulphur centres by studying their oxidation-reduction behaviour during various steady and inhibited states in the light or the dark. We conclude that the Rieske centre is involved in both respiratory and photosynthetic electron transport and is located on the oxygen side of the antimycin A-block. Conversely the HiPIP centre seems to be located on the succinate-cyt. b/c 1 oxido-reductase pathway although apparently in equilibrium with photosynthetic electron transport. We confirm from steady state studies in the wild type our previous analysis of the g=1.94 ferredoxins using mutant strains.
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Zannoni, D., Ingledew, W.J. A functional characterization of the membrane bound iron sulphur centres of Rhodopseudomonas capsulata . Arch Microbiol 135, 176–181 (1983). https://doi.org/10.1007/BF00414475
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DOI: https://doi.org/10.1007/BF00414475