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Cytochrome f: Structure, function and biosynthesis

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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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  1. Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK

    John C. Gray

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Gray, J.C. Cytochrome f: Structure, function and biosynthesis. Photosynth Res 34, 359–374 (1992). https://doi.org/10.1007/BF00029811

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