Cytochrome f: Structure,function and biosynthesis |
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Authors: | John C. Gray |
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Affiliation: | (1) Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA Cambridge, UK |
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Abstract: | Cytochrome f is an intrinsic membrane component of the cytochrome bf complex, transferring electrons from the Rieske FeS protein to plastocyanin in the thylakoid lumen. The protein is held in the thylakoid membrane by a single transmembrane span located near its C-terminus with a globular hydrophilic domain extending into the lumen. The globular domain of the turnip protein has recently been crystallised, offering the prospect of a detailed three-dimensional structure. Reaction with plastocyanin involves localised positive charges on cytochrome f interacting with the acidic patch on plastocyanin and electron transfer via the surface-exposed tyrosine residue (Tyr83) of plastocyanin. Apocytochrome f is encoded in the chloroplast genome and is synthesised with an N-terminal presequence which targets the protein to the thylakoid membrane. The synthesis of cytochrome f is coordinated with the synthesis of the other subunits of the cytochrome bf complex. |
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Keywords: | chloroplast cytochrome bf complex electron transfer petA gene plastocyanin thylakoid membrane protein |
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