| pubmed-article:20211622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20211622 | lifeskim:mentions | umls-concept:C0599132 | lld:lifeskim |
| pubmed-article:20211622 | lifeskim:mentions | umls-concept:C0085403 | lld:lifeskim |
| pubmed-article:20211622 | lifeskim:mentions | umls-concept:C1709375 | lld:lifeskim |
| pubmed-article:20211622 | lifeskim:mentions | umls-concept:C1711411 | lld:lifeskim |
| pubmed-article:20211622 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:20211622 | lifeskim:mentions | umls-concept:C0053241 | lld:lifeskim |
| pubmed-article:20211622 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:20211622 | pubmed:dateCreated | 2010-4-12 | lld:pubmed |
| pubmed-article:20211622 | 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). | lld:pubmed |
| pubmed-article:20211622 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20211622 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20211622 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20211622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20211622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20211622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20211622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20211622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20211622 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:20211622 | pubmed:issn | 1873-3468 | lld:pubmed |
| pubmed-article:20211622 | pubmed:author | pubmed-author:WatanabeTadas... | lld:pubmed |
| pubmed-article:20211622 | pubmed:author | pubmed-author:TomoTatsuyaT | lld:pubmed |
| pubmed-article:20211622 | pubmed:author | pubmed-author:KatoYukiY | lld:pubmed |
| pubmed-article:20211622 | pubmed:author | pubmed-author:YamazakiTakuy... | lld:pubmed |
| pubmed-article:20211622 | pubmed:author | pubmed-author:NagaoRyoR | lld:pubmed |
| pubmed-article:20211622 | pubmed:author | pubmed-author:ShibamotoTada... | lld:pubmed |
| pubmed-article:20211622 | pubmed:copyrightInfo | Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:20211622 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20211622 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:20211622 | pubmed:volume | 584 | lld:pubmed |
| pubmed-article:20211622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20211622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20211622 | pubmed:pagination | 1526-30 | lld:pubmed |
| pubmed-article:20211622 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:meshHeading | pubmed-meshheading:20211622... | lld:pubmed |
| pubmed-article:20211622 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20211622 | pubmed:articleTitle | Species-dependence of the redox potential of the primary quinone electron acceptor QA in photosystem II verified by spectroelectrochemistry. | lld:pubmed |
| pubmed-article:20211622 | pubmed:affiliation | Institute of Industrial Science, The University of Tokyo, Tokyo, Japan. | lld:pubmed |
| pubmed-article:20211622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20211622 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20211622 | lld:pubmed |
