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- W2046767156 abstract "Cytochrome c6A is a unique dithio-cytochrome of green algae and plants. It has a very similar core structure to that of bacterial and algal cytochromes c6, but is unable to fulfil the same function of transferring electrons from cytochrome f to Photosystem I. A key feature of cytochrome c6A is that its haem midpoint potential is more than 200 mV below that of cytochrome c6 (Em≈+340 mV) despite both cytochromes having histidine and methionine residues as axial haem-iron ligands. One salient difference between the haem pockets is that a valine residue in cytochrome c6A replaces a highly conserved glutamine residue in cytochrome c6. This difference has been probed using site-directed mutagenesis, X-ray crystallography and protein film voltammetry studies. It has been found that the stereochemistry of the glutamine residue within the haem pocket has a destabilizing effect and is responsible for tuning the haem's midpoint potential by over 100 mV. This large effect may have contributed to the evolution of a new biological function for cytochrome c6A." @default.
- W2046767156 created "2016-06-24" @default.
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- W2046767156 date "2008-11-19" @default.
- W2046767156 modified "2023-10-01" @default.
- W2046767156 title "Cytochrome c6A: discovery, structure and properties responsible for its low haem redox potential" @default.
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- W2046767156 doi "https://doi.org/10.1042/bst0361175" @default.
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