Source:http://linkedlifedata.com/resource/pubmed/id/20211622
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2010-4-12
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pubmed:abstractText |
The redox potentials E(m)(Q(A)/Q(A)(-)) of the primary quinone electron acceptor Q(A) in oxygen-evolving photosystem II complexes of three species were determined by spectroelectrochemistry. The E(m)(Q(A)/Q(A)(-)) values were experimentally found to be -162+/-3 mV for a higher plant spinach, -171+/-3 mV for a green alga Chlamydomonas reinhardtii and -104+/-4 mV vs. SHE for a red alga Cyanidioschyzon merolae. On the basis of possible deviations for the experimental values, as estimated to differ by 9-29 mV from each true value, plausible causes for such remarkable species-dependence of E(m)(Q(A)/Q(A)(-)) are discussed, mainly by invoking the effects of extrinsic subunits on the delicate structural environment around Q(A).
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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 |
1873-3468
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
16
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pubmed:volume |
584
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1526-30
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:20211622-Benzoquinones,
pubmed-meshheading:20211622-Chlamydomonas reinhardtii,
pubmed-meshheading:20211622-Electrochemistry,
pubmed-meshheading:20211622-Electron Transport,
pubmed-meshheading:20211622-Oxidation-Reduction,
pubmed-meshheading:20211622-Oxygen,
pubmed-meshheading:20211622-Photosystem II Protein Complex,
pubmed-meshheading:20211622-Rhodophyta,
pubmed-meshheading:20211622-Species Specificity,
pubmed-meshheading:20211622-Spectrometry, Fluorescence,
pubmed-meshheading:20211622-Spinacia oleracea
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pubmed:year |
2010
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pubmed:articleTitle |
Species-dependence of the redox potential of the primary quinone electron acceptor QA in photosystem II verified by spectroelectrochemistry.
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pubmed:affiliation |
Institute of Industrial Science, The University of Tokyo, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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