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Cytochrome b6-f complex subunit petO Chloroplastic cytochrome b6-f complex subunit petO (or PETO), also called cytochrome b6-f complex subunit V (suV) or cytochrome b6-f-associated phosphoprotein, is a novel cytochrome b6-f subunit specific in green algae that is predicted by sequence analysis and biochemical characterization to have a one transmembrane alpha-helix topology with two large hydrophilic domains extending on the stromal and lumenal side of the thylakoid membranes, with a lumenal location of the N-terminus. It is reversibly phosphorylated upon state transition, and may have a possible role in signal transduction during redox-controlled short term and long term adaptation of the eukaryotic photosynthetic apparatus. PetO has been shown to contribute to the cyclic electron flow (CEF) around photosystem I (PSI) and cytochrome b6-f that generates ATP.
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