| pubmed-article:2154255 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2154255 | lifeskim:mentions | umls-concept:C0041536 | lld:lifeskim |
| pubmed-article:2154255 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:2154255 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:2154255 | lifeskim:mentions | umls-concept:C1260969 | lld:lifeskim |
| pubmed-article:2154255 | lifeskim:mentions | umls-concept:C0053241 | lld:lifeskim |
| pubmed-article:2154255 | lifeskim:mentions | umls-concept:C0243072 | lld:lifeskim |
| pubmed-article:2154255 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2154255 | pubmed:dateCreated | 1990-3-26 | lld:pubmed |
| pubmed-article:2154255 | pubmed:abstractText | The effect of substituents on the 1,4-benzoquinone ring of ubiquinone on its electron-transfer activity in the bovine heart mitochondrial succinate-cytochrome c reductase region is studied by using synthetic ubiquinone derivatives that have a decyl (or geranyl) side-chain at the 6-position and various arrangements of methyl, methoxy and hydrogen in the 2, 3 and 5 positions of the benzoquinone ring. The reduction of quinone derivatives by succinate is measured with succinate-ubiquinone reductase and with succinate-cytochrome c reductase. Oxidation of quinol derivatives is measured with ubiquinol-cytochrome c reductase. The electron-transfer efficacy of quinone derivatives is compared to that of 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone. When quinone derivatives are used as the electron acceptor for succinate-ubiquinone reductase, the methyl group at the 5-position is less important than are the methoxy groups at the 2- and 3-positions. Replacing the 5-methyl group with hydrogen causes a slight increase in activity. However, replacing one or both of 2- and 3-methoxy groups with a methyl completely abolishes electron-acceptor activity. Replacing the 3-methoxy group with hydrogen results in a complete loss of electron-acceptor activity, while replacing the 2-methoxy with hydrogen results in an activity decrease by 70%, suggesting that the methoxy group at the 3-position is more specific than that at the 2-position. The structural requirements for quinol derivatives to be oxidized by ubiquinol-cytochrome c reductase are less strict. All 1,4-benzoquinol derivatives examined show partial activity when used as electron donors for ubiquinol-cytochrome c reductase. Derivatives that possess one unsubstituted position at 2, 3 or 5, with a decyl group at the 6-position, show substrate inhibition at high concentrations. Such substrate inhibition is not observed when fully substituted derivatives are used. The structural requirements for quinone derivatives to be reduced by succinate-cytochrome c reductase are less specific than those for succinate-ubiquinone reductase. Replacing one or both of the 2- and 3-methoxy groups with a methyl and keeping the 5-position unsubstituted (plastoquinone derivatives) yields derivatives with no acceptor activity for succinate-Q reductase. However, these derivatives are reducible by succinate in the presence of succinate-cytochrome c reductase. This reduction is antimycin-sensitive and requires endogenous ubiquinone, suggesting that these (plastoquinone) derivatives can only accept electrons from the ubisemiquinone radical at the Qi site of ubiquinol-cytochrome c reductase, and cannot accept electrons from the QPs of succinate-ubiquinone reductase. | lld:pubmed |
| pubmed-article:2154255 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2154255 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2154255 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2154255 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2154255 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:2154255 | pubmed:author | pubmed-author:YuLL | lld:pubmed |
| pubmed-article:2154255 | pubmed:author | pubmed-author:YuC ACA | lld:pubmed |
| pubmed-article:2154255 | pubmed:author | pubmed-author:GuL QLQ | lld:pubmed |
| pubmed-article:2154255 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2154255 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:2154255 | pubmed:volume | 1015 | lld:pubmed |
| pubmed-article:2154255 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2154255 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2154255 | pubmed:pagination | 482-92 | lld:pubmed |
| pubmed-article:2154255 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2154255 | pubmed:meshHeading | pubmed-meshheading:2154255-... | lld:pubmed |
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| pubmed-article:2154255 | pubmed:meshHeading | pubmed-meshheading:2154255-... | lld:pubmed |
| pubmed-article:2154255 | pubmed:meshHeading | pubmed-meshheading:2154255-... | lld:pubmed |
| pubmed-article:2154255 | pubmed:meshHeading | pubmed-meshheading:2154255-... | lld:pubmed |
| pubmed-article:2154255 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2154255 | pubmed:articleTitle | Effect of substituents of the benzoquinone ring on electron-transfer activities of ubiquinone derivatives. | lld:pubmed |
| pubmed-article:2154255 | pubmed:affiliation | Department of Biochemistry, OAES, Oklahoma State University, Stillwater 74078. | lld:pubmed |
| pubmed-article:2154255 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2154255 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2154255 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2154255 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
