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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1995-7-20
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pubmed:abstractText |
Functional identity and significant similarities in cofactors and sequence exist between the L and M reaction center proteins of the photosynthetic bacteria and the D1 and D2 photosystem-II reaction center proteins of cyanobacteria, algae, and plants. A model of the quinone (QB) binding site of the D1 protein is presented based upon the resolved structure of the QB binding pocket of the L subunit, and introducing novel quantitative notions of complementarity and contact surface between atoms. This model, built without using traditional methods of molecular mechanics and restricted to residues in direct contact with QB, accounts for the experimentally derived functional state of mutants of the D1 protein in the region of QB. It predicts the binding of both the classical and phenol-type PSII herbicides and rationalizes the relative levels of tolerance of mutant phenotypes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Atrazine,
http://linkedlifedata.com/resource/pubmed/chemical/Diuron,
http://linkedlifedata.com/resource/pubmed/chemical/Herbicides,
http://linkedlifedata.com/resource/pubmed/chemical/Iodobenzenes,
http://linkedlifedata.com/resource/pubmed/chemical/Nitriles,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Photosystem II Protein Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Plastoquinone,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/Triazines,
http://linkedlifedata.com/resource/pubmed/chemical/ioxynil
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0887-3585
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
214-25
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7784425-Atrazine,
pubmed-meshheading:7784425-Binding, Competitive,
pubmed-meshheading:7784425-Binding Sites,
pubmed-meshheading:7784425-Chemistry, Physical,
pubmed-meshheading:7784425-Diuron,
pubmed-meshheading:7784425-Herbicides,
pubmed-meshheading:7784425-Iodobenzenes,
pubmed-meshheading:7784425-Mathematics,
pubmed-meshheading:7784425-Models, Molecular,
pubmed-meshheading:7784425-Nitriles,
pubmed-meshheading:7784425-Phenotype,
pubmed-meshheading:7784425-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:7784425-Photosystem II Protein Complex,
pubmed-meshheading:7784425-Physicochemical Phenomena,
pubmed-meshheading:7784425-Plastoquinone,
pubmed-meshheading:7784425-Protein Conformation,
pubmed-meshheading:7784425-Quinones,
pubmed-meshheading:7784425-Rhodopseudomonas,
pubmed-meshheading:7784425-Substrate Specificity,
pubmed-meshheading:7784425-Triazines
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pubmed:year |
1995
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pubmed:articleTitle |
Modeling the quinone-B binding site of the photosystem-II reaction center using notions of complementarity and contact-surface between atoms.
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pubmed:affiliation |
Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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