NDLI: Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover.

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Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover.

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Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Feher, G. Paddock, M. L. Okamura, M. Y. Rongey, S. H.
Description	Author Affiliation: Paddock ML ( Department of Physics, University of California, San Diego, La Jolla 92093.);
Abstract	The mechanism of proton transfer in the reaction centers (RCs) from Rhodobacter sphaeroides was investigated by site-directed mutagenesis. Replacement of Glu-212 of the L subunit, a protonatable residue located near the secondary acceptor (QB) binding site, by glutamine reduced the in vitro electron turnover from cytochrome c to 2,3-dimethoxy-5-methylbenzoquinone (UQ0) by a factor of 25. The electron transfer rate to QB remained essentially unimpaired. Consequently, it is postulated that the reduced turnover in the mutant is due to a reduced rate of proton transfer to QB2-. The lack of pH dependence of the forward electron transfer rate DQA-QB----DQAQB- and the back reaction rate D+QAQB- ----DQAQB (where D = primary donor and QA = primary acceptor) in the mutant RC indicate that the observed pH dependence in the native RC is due to Glu-212, which has an anomalously high pKa value of 9.5 +/- 0.3. These results support the involvement of Glu-212 as a proton donor to reduced QB.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Metabolism Glutamates Glutamine Mutation Quinones Rhodobacter Sphaeroides Genetics Chromosome Deletion Cytochrome c Group Electron Transport Genes Genes, Bacterial Glutamic Acid Kinetics Models, Molecular Photosynthetic Reaction Center Complex Proteins Protein Conformation Restriction Mapping Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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