Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052916 | FEBS Letters | 2006 | 4 Pages |
Abstract
Cytochrome c6A is a dithio-cytochrome recently discovered in land plants and green algae, and believed to be derived from the well-known cytochrome c6. The function of cytochrome c6A is unclear. We propose that it catalyses the formation of disulphide bridges in thylakoid lumen proteins in a single-step disulphide exchange reaction, with subsequent transfer of the reducing equivalents to plastocyanin. The haem group of cytochrome c6A acts as an electron sink, allowing rapid resolution of a radical intermediate formed during reoxidation of cytochrome c6A. Our model is consistent with previously published data on mutant plants, and the likely evolution of the protein.
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Authors
Beatrix G. Schlarb-Ridley, Robert H. Nimmo, Saul Purton, Christopher J. Howe, Derek S. Bendall,