pubmed-article:3038186 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3038186 | lifeskim:mentions | umls-concept:C0038615 | lld:lifeskim |
pubmed-article:3038186 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
pubmed-article:3038186 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:3038186 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
pubmed-article:3038186 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:3038186 | pubmed:dateCreated | 1987-9-23 | lld:pubmed |
pubmed-article:3038186 | pubmed:abstractText | Antimycin-insensitive succinate-cytochrome c reductase activity has been detected in pure, reconstitutively active succinate dehydrogenase. The enzyme catalyzes electron transfer from succinate to cytochrome c at a rate of 0.7 mumole succinate oxidized per min per mg protein, in the presence of 100 microM cytochrome c. This activity, which is about 2% of that of reconstitutive (the ability of succinate dehydrogenase to reconstitute with coenzyme ubiquinone-binding proteins (QPs) to form succinate-ubiquinone reductase) or succinate-phenazine methosulfate activity in the preparation, differs from antimycin-insensitive succinate-cytochrome c reductase activity detected in submitochondrial particles or isolated succinate-cytochrome c reductase. The Km for cytochrome c for the former is too high to be measured. The Km for the latter is about 4.4 microM, similar to that of antimycin-sensitive succinate-cytochrome c activity in isolated succinate-cytochrome c reductase, suggesting that antimycin-insensitive succinate-cytochrome c activity of succinate-cytochrome c reductase probably results from incomplete inhibition by antimycin. Like reconstitutive activity of succinate dehydrogenase, the antimycin-insensitive succinate-cytochrome c activity of succinate dehydrogenase is sensitive to oxygen; the half-life is about 20 min at 0 degrees C at a protein concentration of 23 mg/ml. In the presence of QPs, the antimycin-insensitive succinate-cytochrome c activity of succinate dehydrogenase disappears and at the same time a thenoyltrifluoroacetone-sensitive succinate-ubiquinone reductase activity appears. This suggests that antimycin-insensitive succinate-cytochrome c reductase activity of succinate dehydrogenase appears when succinate dehydrogenase is detached from the membrane or from QPs. Reconstitutively active succinate dehydrogenase oxidizes succinate using succinylated cytochrome c as electron acceptor, suggesting that a low potential intermediate (radical) may be involved. This suggestion is confirmed by the detection of an unknown radical by spin trapping techniques. When a spin trap, alpha-phenyl-N-tert-butylnitrone (PBN), is added to a succinate oxidizing system containing reconstitutively active succinate dehydrogenase, a PBN spin adduct is generated. Although this PBN spin adduct is identical to that generated by xanthine oxidase, indicating that a perhydroxy radical might be involved, the insensitivity of this antimycin-insensitive succinate-cytochrome c reductase activity to superoxide dismutase and oxygen questions the nature of this observed radical. | lld:pubmed |
pubmed-article:3038186 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:language | eng | lld:pubmed |
pubmed-article:3038186 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3038186 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3038186 | pubmed:month | Aug | lld:pubmed |
pubmed-article:3038186 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:3038186 | pubmed:author | pubmed-author:YuLL | lld:pubmed |
pubmed-article:3038186 | pubmed:author | pubmed-author:YuC ACA | lld:pubmed |
pubmed-article:3038186 | pubmed:author | pubmed-author:McCurleyJ PJP | lld:pubmed |
pubmed-article:3038186 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3038186 | pubmed:day | 12 | lld:pubmed |
pubmed-article:3038186 | pubmed:volume | 893 | lld:pubmed |
pubmed-article:3038186 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3038186 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3038186 | pubmed:pagination | 75-82 | lld:pubmed |
pubmed-article:3038186 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:3038186 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3038186 | pubmed:articleTitle | An antimycin-insensitive succinate-cytochrome c reductase activity in pure reconstitutively active succinate dehydrogenase. | lld:pubmed |
pubmed-article:3038186 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3038186 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3038186 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:3038186 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |