Species differences in unlocking B‐side electron transfer in bacterial reaction centers
Open Access
- 21 June 2016
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 590 (16) , 2515-2526
Abstract
The structure of the bacterial photosynthetic reaction center (RC) reveals symmetry‐related electron transfer (ET) pathways, but only one path is used in native RCs. Analogous mutations have been made in two Rhodobacter (R.) species. A glutamic acid at position 133 in the M subunit increases transmembrane charge separation via the naturally inactive (B‐side) path through impacts on primary ET in mutant R. sphaeroidesRCs. Prior work showed that the analogous substitution in the R. capsulatusRC also increases B‐side activity, but mainly affects secondary ET. The overall yields of transmembrane ET are similar, but enabled in fundamentally different ways.Keywords
Funding Information
- U.S. Department of Energy
- Office of Science
- National Science Foundation (DGE‐1143954)
This publication has 65 references indexed in Scilit:
- Optimizing multi-step B-side charge separation in photosynthetic reaction centers from Rhodobacter capsulatusBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2016
- High Throughput Engineering to Revitalize a Vestigial Electron Transfer Pathway in Bacterial Photosynthetic Reaction CentersJournal of Biological Chemistry, 2012
- Rewiring photosynthesis: engineering wrong-way electron transfer in the purple bacterial reaction centreBiochemical Society Transactions, 2005
- Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 å resolution: cofactors and protein-cofactor interactionsStructure, 1994
- Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroidesBiochemistry, 1991
- Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits.Proceedings of the National Academy of Sciences, 1987
- Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors.Proceedings of the National Academy of Sciences, 1987
- Primary photochemistry of reaction centers from the photosynthetic purple bacteriaPhotosynthesis Research, 1987
- Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolutionNature, 1985
- Chromosomal deletion and plasmid complementation of the photosynthetic reaction center and light-harvesting genes from Rhodopseudomonas capsulataGene, 1985