| pubmed-article:8546703 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8546703 | lifeskim:mentions | umls-concept:C2245017 | lld:lifeskim |
| pubmed-article:8546703 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:8546703 | lifeskim:mentions | umls-concept:C0041536 | lld:lifeskim |
| pubmed-article:8546703 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:8546703 | pubmed:dateCreated | 1996-2-14 | lld:pubmed |
| pubmed-article:8546703 | pubmed:abstractText | We report the first detailed study on the ubiquinone (coenzyme Q; abbreviated to Q) analogue specificity of mitochondrial complex I, NADH:Q reductase, in intact submitochondrial particles. The enzymic function of complex I has been investigated using a series of analogues of Q as electron acceptor substrates for both electron transport activity and the associated generation of membrane potential. Q analogues with a saturated substituent of one to three carbons at position 6 of the 2,3-dimethoxy-5-methyl-1,4-benzoquinone ring have the fastest rates of electron transport activity, and analogues with a substituent of seven to nine carbon atoms have the highest values of association constant derived from NADH:Q reductase activity. The rate of NADH:Q reductase activity is potently but incompletely inhibited by rotenone, and the residual rotenone-insensitive rate is stimulated by Q analogues in different ways depending on the hydrophobicity of their substituent. Membrane potential measurements have been undertaken to evaluate the energetic efficiency of complex I with various Q analogues. Only hydrophobic analogues such as nonyl-Q or undecyl-Q show an efficiency of membrane potential generation equivalent to that of endogenous Q. The less hydrophobic analogues as well as the isoprenoid analogue Q-2 are more efficient as substrates for the redox activity of complex I than for membrane potential generation. Thus the hydrophilic Q analogues act also as electron sinks and interact incompletely with the physiological Q site in complex I that pumps protons and generates membrane potential. | lld:pubmed |
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| pubmed-article:8546703 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8546703 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8546703 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8546703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8546703 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8546703 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8546703 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:LinnaneA WAW | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:Degli... | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:GhelliAA | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:RattiEE | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:NgoAA | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:McMullenG LGL | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:BenelliBB | lld:pubmed |
| pubmed-article:8546703 | pubmed:author | pubmed-author:SparlaFF | lld:pubmed |
| pubmed-article:8546703 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8546703 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8546703 | pubmed:volume | 313 ( Pt 1) | lld:pubmed |
| pubmed-article:8546703 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8546703 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8546703 | pubmed:pagination | 327-34 | lld:pubmed |
| pubmed-article:8546703 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8546703 | pubmed:meshHeading | pubmed-meshheading:8546703-... | lld:pubmed |
| pubmed-article:8546703 | pubmed:year | 1996 | lld:pubmed |
