Binding of cytochrome c to the cytochrome bc1 complex (complex III) and its subunits cytochrome c1 and b1. |
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Authors: | H.R. Bosshard M. Zürrer H. Schägger G. von Jagow |
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Affiliation: | 1. Biochemisches Institut der Universität, CH-8028 Zürich, Switzerland;2. Institut für Physiologische Chemie und Physikalische Biochemie der Universität, Goethestrasse 33, D-8000 München 2 G.F.R. |
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Abstract: | Cytochrome 1, the electron donor for cytochrome , is a subunit of the mitochondrial cytochrome 1 complex (complex III, cytochrome reductase). To test if cytochrome 1 is the cytochrome -binding subunit of the 1 complex, binding of cytochrome to the complex and to isolated cytochrome 1 was compared by a gel-filtration method under non-equilibrium conditions (a 1 complex lacking the Rieske ironsulfur protein was used; von Jagow et al. (1977) Biochim. Biophys. Acta , 549–558). The approximate stoichiometries and binding affinities were found to be very similar. Binding of cytochrome to isolated cytochrome which is another subunit of the reductase was not detectable by the gel-filtration method. Further, the same lysine residues of cytochrome were shielded towards chemical acetylation in the complexes 1 and 1. From this we conclude that the same surface area of cytochrome is in direct contact with cytochrome 1 and with cytochrome 1 in the respective complexes and that therefore cytochrome is most probably the structural ligand for cytochrome in mitochondrial cytochrome reductase. |
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Keywords: | To whom to address correspondence. |
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