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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-6-23
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pubmed:abstractText |
Flash-induced absorption spectroscopy has been used to characterize Rhodobacter capsulatus reaction centers mutated in the secondary quinone acceptor site (Q(B). We compared the wild-type, the L212Glu-L213Asp --> Ala-Ala photosynthetically incompetent double mutant (DM), and two photocompetent revertants, the DM+L217Arg --> Cys and the DM+M5Asn- --> Asp strains. The electrostatic environment for Q(B)- is different in the two revertant strains. Only the L217Arg --> Cys mutation nearly restores the native electrostatic environment of Q(B)-. However, the level of recovery of the reaction center function, measured by the rates of second electron transfer and cytochrome c turnover, is quite incomplete in both strains. This shows that a wild-type-like electrostatic environment of Q(B)- cannot ensure on its own, rapid and efficient proton transfer to Q(B)-.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
407
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
159-63
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9166891-Cytochrome c Group,
pubmed-meshheading:9166891-Electron Transport,
pubmed-meshheading:9166891-Light,
pubmed-meshheading:9166891-Mutation,
pubmed-meshheading:9166891-Oxidation-Reduction,
pubmed-meshheading:9166891-Photosynthesis,
pubmed-meshheading:9166891-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:9166891-Protons,
pubmed-meshheading:9166891-Quinones,
pubmed-meshheading:9166891-Rhodobacter capsulatus,
pubmed-meshheading:9166891-Spectrophotometry,
pubmed-meshheading:9166891-Static Electricity,
pubmed-meshheading:9166891-Thermodynamics
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pubmed:year |
1997
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pubmed:articleTitle |
A native electrostatic environment near Q(B) is not sufficient to ensure rapid proton delivery in photosynthetic reaction centers.
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pubmed:affiliation |
Centre de Génétique Moléculaire, CNRS, Gif/Yvette, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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