| pubmed-article:7988549 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0596972 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0035495 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0812406 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C2755839 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0037812 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C1521743 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0181904 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C1704646 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0728873 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0282183 | lld:lifeskim |
| pubmed-article:7988549 | lifeskim:mentions | umls-concept:C0332514 | lld:lifeskim |
| pubmed-article:7988549 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:7988549 | pubmed:dateCreated | 1995-1-9 | lld:pubmed |
| pubmed-article:7988549 | pubmed:abstractText | Using 1-, 2-, 3- and 4-13C site-specifically labelled ubiquinone-10, reconstituted at the QA site of Rhodobacter sphaeroides R26 reaction centres, the infra-red bands dominated by the 1- and 4-C = O vibration of QA are assigned in the QA(-)-QA difference spectra. The mode dominated by the 4-C = O vibration is drastically downshifted in the reaction centres as compared with its absorption frequency in free ubiquinone-10. In contrast, the mode dominated by the 1-C = O vibration absorbs at similar frequencies in the free and the bound forms. The frequency shift of the 4-C = O vibration is due to a large decrease in bond order and indicates a strong interaction with the protein microenvironment in the ground state. In the charge-separated state the mode dominated by the semiquinone 4-C = O vibration is characteristic of strong hydrogen bonding to the microenvironment, whereas the mode dominated by the 1-C = O vibration indicates a weaker interaction. The asymmetric binding of the 1- and 4-C = O groups to the protein might contribute to the factors governing different redox reactions of ubiquinone-10 at the QA site as compared with its reactions at the QB site. | lld:pubmed |
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| pubmed-article:7988549 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7988549 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7988549 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7988549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7988549 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7988549 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7988549 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:LINDR MRM | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:GaryJJ | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:LugtenburgJJ | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:GerwertKK | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:de GrootH JHJ | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:van LiemtW... | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:BrudlerRR | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:SteggerdaW... | lld:pubmed |
| pubmed-article:7988549 | pubmed:author | pubmed-author:EsmeijerRR | lld:pubmed |
| pubmed-article:7988549 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7988549 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7988549 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:7988549 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7988549 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7988549 | pubmed:pagination | 5523-30 | lld:pubmed |
| pubmed-article:7988549 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
| pubmed-article:7988549 | pubmed:meshHeading | pubmed-meshheading:7988549-... | lld:pubmed |
| pubmed-article:7988549 | pubmed:meshHeading | pubmed-meshheading:7988549-... | lld:pubmed |
| pubmed-article:7988549 | pubmed:meshHeading | pubmed-meshheading:7988549-... | lld:pubmed |
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| pubmed-article:7988549 | pubmed:meshHeading | pubmed-meshheading:7988549-... | lld:pubmed |
| pubmed-article:7988549 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7988549 | pubmed:articleTitle | Asymmetric binding of the 1- and 4-C=O groups of QA in Rhodobacter sphaeroides R26 reaction centres monitored by Fourier transform infra-red spectroscopy using site-specific isotopically labelled ubiquinone-10. | lld:pubmed |
| pubmed-article:7988549 | pubmed:affiliation | Institut für Biophysik, Ruhr-Universität Bochum. | lld:pubmed |
| pubmed-article:7988549 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7988549 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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