Amino acid identities in the three redox center-carrying polypeptides of cytochromebc 1/b 6 f complexes |
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Authors: | G. Hauska W. Nitschke R. G. Herrmann |
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Affiliation: | (1) Institut für Botanik, Universität Regensburg, Universitätsstrasse 31, D-8400 Regensburg, FRG;(2) Botanisches Institut der Ludwig-Maximilians-Universität, Menzingerstrasse 67, D-800 München 19, FRG |
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Abstract: | The comparison of primary structures is extended to 22 cytochromesb orb6, 12 cytochromesc1 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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Keywords: | Cytochromebc1 complex cytochromeb6f complex Rieske FeS protein amino acid sequences quinone-binding peptides membrane proteins organelle gene evolution |
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