An atypical haem in the cytochrome b6f complex

David Stroebel, Yves Choquet, Jean-Luc Popot () and Daniel Picot ()
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David Stroebel: CNRS/Université
Yves Choquet: CNRS UPR 1261, Institut de Biologie Physico-Chimique
Jean-Luc Popot: CNRS/Université
Daniel Picot: CNRS/Université

Nature, 2003, vol. 426, issue 6965, 413-418

Abstract: Abstract Photosystems I and II (PSI and II) are reaction centres that capture light energy in order to drive oxygenic photosynthesis; however, they can only do so by interacting with the multisubunit cytochrome b6f complex. This complex receives electrons from PSII and passes them to PSI, pumping protons across the membrane and powering the Q-cycle. Unlike the mitochondrial and bacterial homologue cytochrome bc1, cytochrome b6f can switch to a cyclic mode of electron transfer around PSI using an unknown pathway. Here we present the X-ray structure at 3.1 Å of cytochrome b6f from the alga Chlamydomonas reinhardtii. The structure bears similarities to cytochrome bc1 but also exhibits some unique features, such as binding chlorophyll, β-carotene and an unexpected haem sharing a quinone site. This haem is atypical as it is covalently bound by one thioether linkage and has no axial amino acid ligand. This haem may be the missing link in oxygenic photosynthesis.

Date: 2003
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DOI: 10.1038/nature02155

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