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Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 41))

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Summary

Cytochrome c 6A must be an important protein, as it is conserved across plant and green algal lineages, yet its function remains as mysterious as when it was discovered over 10 years ago. The protein is similar in sequence to conventional cytochrome c 6 proteins, which are well known as alternatives to plastocyanin in transferring electrons from the cytochrome b 6 f complex to Photosystem I in the light reactions of photosynthesis. Yet cytochrome c 6A has a dramatically lower redox midpoint potential than conventional cytochrome c 6, meaning that it is an unsuitable electron acceptor from cytochrome f. The structure of cytochrome c 6A has been determined, and mutagenesis studies have pinpointed a single substitution compared to cytochrome c 6 that is responsible for at least 100 mV of the lowering of the midpoint potential—a remarkable effect for a single residue. Another striking feature of cytochrome c 6A, absent from cytochrome c 6, is a 12-residue insertion in a loop region of the protein. This insertion has two conserved cysteine residues. The function of these is unknown, but may be structural rather than catalytic. Cytochrome c 6A is able to transfer electrons to plastocyanin. Transcriptomic and proteomic studies have provided remarkably little insight into the protein’s function. Ironically, the recognition of cytochrome c 6A in plants—from which cytochrome c 6 was long thought to be absent—has now led to the recognition of a previously unsuspected class of cytochrome c 6-like proteins in cyanobacteria, designated cytochrome c 6B and cytochrome c 6C.

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Abbreviations

LIP:

Loop insertion peptide

pI :

Isoelectric point

PPI:

Peptidyl-prolyl cis-trans isomerase

PS I:

Photosystem I

PS II:

Photosystem II

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Acknowledgements

We are grateful to the Biotechnology and Biological Sciences Research Council, the Leverhulme Trust, and the European Commission for their support of our work on this protein.

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Correspondence to Christopher J. Howe .

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Howe, C.J., Nimmo, R.H., Barbrook, A.C., Bendall, D.S. (2016). Cytochrome c 6A of Chloroplasts. In: Cramer, W., Kallas, T. (eds) Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling. Advances in Photosynthesis and Respiration, vol 41. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-7481-9_33

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