Abstract
The cytochrome b-f complex of the chloroplast thylakoid membrane operates as a plastoquinol/plastocyanin oxido-reductase and is thus analogous to the mitochondrial cytochrome bc 1 complex with which it bears a large amount of structural and functional similarity1 It consists of four components, which are cytochrome f, cytochrome b-563, the Rieske Fe-S protein, and a 17kDa protein (subunit IV). In addition a number of small (~5kDa) have been suggested to be part of the complex2, though this requires confirmation. The Rieske Fe-S protein may be removed from the isolated complex by hydroxyapatite chromatography in the presence of Triton X-1003 and may be identified by a characteristic EPR signal4 as well as by a size of 20kDa on SDS-PAGE.
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