| pubmed-article:4320 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4320 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:4320 | lifeskim:mentions | umls-concept:C0038615 | lld:lifeskim |
| pubmed-article:4320 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
| pubmed-article:4320 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:4320 | pubmed:dateCreated | 1976-7-6 | lld:pubmed |
| pubmed-article:4320 | pubmed:abstractText | Soluble succinate dehydrogenase prepared by butanol extraction reacts with N-ethylmaleimide according to first-order kinetics with respect to both remaining active enzyme and the inhibitor concentration. Binding of the sulfhydryl groups of the enzyme prevents its alkylation by N-ethylmaleimide and inhibition by oxaloacetate. A kinetic analysis of the inactivation of alkylating reagent in the presence of succinate or malonate suggests that N-ethylmaleimide acts as a site-directed inhibitor. The apparent first-order rate constant of alkylation increases between pH 5.8 and 7.8 indicating a pKa value for the enzyme sulfhydryl group equal to 7.0 at 22 degrees C in 50 mM Tris-sufate buffer. Certain anions (phosphate, citrate, maleate and acetate) decrease the reactivity of the enzyme towards the alkylating reagent. Succinate/phenazine methosulfate reductase activity measured in the presence of a saturating concentration of succinate shows the same pH-dependence as the alkylation rate by N-ethylmaleimide. The mechanism of the first step of succinate oxidation, including a nucleophilic attack of substrate by the active-site sulfhydryl group, is discussed. | lld:pubmed |
| pubmed-article:4320 | pubmed:language | eng | lld:pubmed |
| pubmed-article:4320 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4320 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:4320 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4320 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4320 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4320 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4320 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4320 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4320 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:4320 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:4320 | pubmed:author | pubmed-author:VinogradovA... | lld:pubmed |
| pubmed-article:4320 | pubmed:author | pubmed-author:GavrikovaE... | lld:pubmed |
| pubmed-article:4320 | pubmed:author | pubmed-author:ZuevskyV VVV | lld:pubmed |
| pubmed-article:4320 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4320 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:4320 | pubmed:volume | 63 | lld:pubmed |
| pubmed-article:4320 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4320 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4320 | pubmed:pagination | 365-71 | lld:pubmed |
| pubmed-article:4320 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Hyd... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Sul... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Mal... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Mat... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Suc... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Suc... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Kin... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Pro... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Sol... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Eth... | lld:pubmed |
| pubmed-article:4320 | pubmed:meshHeading | pubmed-meshheading:4320-Bin... | lld:pubmed |
| pubmed-article:4320 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:4320 | pubmed:articleTitle | Reactivity of the sulfhydryl groups of soluble succinate dehydrogenase. | lld:pubmed |
| pubmed-article:4320 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4320 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4320 | lld:pubmed |
