Abstract
The cytochrome b-f complex of the chloroplast thylakoid membrane operates as a plastoquinol-plastocyanin oxidoreductase and is thus analogous to the mitochondrial cytochrome bc 1 complex with which it bears a large amount of structural and functional similarity. It consists in all higher plants of four components, which are cytochrome f, cytochrome b-563 the Rieske Fe-S protein, and a 17kDa protein (subunit IV)1. The cytochrome b-f complex has also been reported to contain small polypeptides1 and a chloroplast-encoded 5kDa polypeptide has recently been identified in maize and spinach2.The 20 kDa Rieske Fe-S protein may be removed from the isolated complex by hydroxyapatite chromatography in the presence of Triton X-1003.
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