Source:http://linkedlifedata.com/resource/pubmed/id/15865437
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
2005-5-3
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pubmed:databankReference | |
pubmed:abstractText |
The photosynthetic reaction center (RC) from purple bacteria converts light into chemical energy. Although the RC shows two nearly structurally symmetric branches, A and B, light-induced electron transfer in the native RC occurs almost exclusively along the A-branch to a primary quinone electron acceptor Q(A). Subsequent electron and proton transfer to a mobile quinone molecule Q(B) converts it to a quinol, Q(B)H(2). We report the construction and characterization of a series of mutants in Rhodobacter sphaeroides designed to reduce Q(B) via the B-branch. The quantum efficiency to Q(B) via the B-branch Phi(B) ranged from 0.4% in an RC containing the single mutation Ala-M260 --> Trp to 5% in a quintuple mutant which includes in addition three mutations to inhibit transfer along the A-branch (Gly-M203 --> Asp, Tyr-M210 --> Phe, Leu-M214 --> His) and one to promote transfer along the B-branch (Phe-L181 --> Tyr). Comparing the value of 0.4% for Phi(B) obtained in the AW(M260) mutant, which lacks Q(A), to the 100% quantum efficiency for Phi(A) along the A-branch in the native RC, we obtain a ratio for A-branch to B-branch electron transfer of 250:1. We determined the structure of the most effective (quintuple) mutant RC at 2.25 A (R-factor = 19.6%). The Q(A) site did not contain a quinone but was occupied by the side chain of Trp-M260 and a Cl(-). In this structure a nonfunctional quinone was found to occupy a new site near M258 and M268. The implications of this work to trap intermediate states are discussed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacteriochlorophylls,
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Pheophytins,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/bacteriopheophytin,
http://linkedlifedata.com/resource/pubmed/chemical/benzoquinone
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6920-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15865437-Bacteriochlorophylls,
pubmed-meshheading:15865437-Benzoquinones,
pubmed-meshheading:15865437-Binding Sites,
pubmed-meshheading:15865437-Crystallization,
pubmed-meshheading:15865437-Crystallography, X-Ray,
pubmed-meshheading:15865437-Electron Transport,
pubmed-meshheading:15865437-Kinetics,
pubmed-meshheading:15865437-Lasers,
pubmed-meshheading:15865437-Models, Chemical,
pubmed-meshheading:15865437-Mutagenesis, Site-Directed,
pubmed-meshheading:15865437-Oxidation-Reduction,
pubmed-meshheading:15865437-Pheophytins,
pubmed-meshheading:15865437-Photolysis,
pubmed-meshheading:15865437-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:15865437-Rhodobacter sphaeroides,
pubmed-meshheading:15865437-Spectrophotometry
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pubmed:year |
2005
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pubmed:articleTitle |
Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure.
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pubmed:affiliation |
Department of Physics, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093, USA. mpaddock@physics.ucsd.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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