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Amino acid identities in the three redox center-carrying polypeptides of cytochromebc 1/b 6 f complexes

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Abstract

The comparison of primary structures is extended to 22 cytochromesb orb 6, 12 cytochromesc 1 orf, and 8 Rieske FeS proteins. Conclusions are drawn as to their phylogenetic relationship as well as on conserved, functionally important amino acids and secondary structures. The results are in favor of two independent quinone binding sites at opposite surfaces of the membrane, topping one of the two hemes of cytochromeb each.

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Authors and Affiliations

  1. Institut für Botanik, Universität Regensburg, Universitätsstrasse 31, D-8400, Regensburg, FRG

    G. Hauska & W. Nitschke

  2. Botanisches Institut der Ludwig-Maximilians-Universität, Menzingerstrasse 67, D-800, München 19, FRG

    R. G. Herrmann

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  1. G. Hauska
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  2. W. Nitschke
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  3. R. G. Herrmann
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Hauska, G., Nitschke, W. & Herrmann, R.G. Amino acid identities in the three redox center-carrying polypeptides of cytochromebc 1/b 6 f complexes. J Bioenerg Biomembr 20, 211–228 (1988). https://doi.org/10.1007/BF00768395

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