The purple bacterial reaction centre uses light energy to separate charge across the cytoplasmic membrane, reducing ubiquinone and oxidizing a c-type cytochrome. The protein possesses a macroscopic structural two-fold symmetry but displays a strong functional asymmetry, with only one of two available membrane-spanning branches of cofactors (the so-called A-branch) being used to catalyse photochemical charge separation. The factors underlying this functional asymmetry have been the subject of study for many years but are still not fully understood. Site-directed mutagenesis has been partially successful in rerouting electron transfer along the normally inactive B-branch, allowing comparison of the kinetics of equivalent electron transfer reactions on the two branches. Both the primary and secondary electron transfer steps on the B-branch appear to be considerably slower than their A-branch counterparts. The effectiveness of different mutations in rerouting electron transfer along the B-branch of cofactors is discussed.
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Conference Article|
August 01 2005
Rewiring photosynthesis: engineering wrong-way electron transfer in the purple bacterial reaction centre
M.C. Wakeham;
M.C. Wakeham
1Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol, BS8 1TD, U.K.
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M.R. Jones
M.R. Jones
1
1Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol, BS8 1TD, U.K.
1To whom correspondence should be addressed (email m.r.jones@bristol.ac.uk).
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Publisher: Portland Press Ltd
Received:
March 31 2005
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2005 The Biochemical Society
2005
Biochem Soc Trans (2005) 33 (4): 851–857.
Article history
Received:
March 31 2005
Citation
M.C. Wakeham, M.R. Jones; Rewiring photosynthesis: engineering wrong-way electron transfer in the purple bacterial reaction centre. Biochem Soc Trans 1 August 2005; 33 (4): 851–857. doi: https://doi.org/10.1042/BST0330851
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