| pubmed-article:6303306 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6303306 | lifeskim:mentions | umls-concept:C0445951 | lld:lifeskim |
| pubmed-article:6303306 | lifeskim:mentions | umls-concept:C0020284 | lld:lifeskim |
| pubmed-article:6303306 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6303306 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:6303306 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6303306 | pubmed:dateCreated | 1983-6-10 | lld:pubmed |
| pubmed-article:6303306 | pubmed:abstractText | The membrane-bound hydrogenase from the anaerobic sulphate-reducing bacterium Desulfovibrio desulfuricans (Norway strain) has been purified to homogeneity, with an overall 80-fold purification and a specific activity of 70 mumol of H2 evolved/min per mg of protein. The hydrogenase had a relative molecular mass of 58 000 as determined by gel filtration and was estimated to contain six iron atoms and six acid-labile sulphur groups per molecule. The absorption spectrum of the enzyme was characteristic of an iron-sulphur protein. The E400 and E280 were 28 500 and 109 000 M-1.cm-1 respectively. The e.s.r. of the oxidized protein indicated the presence of [4Fe-4S]3+ or [3Fe-3S]3+, and another paramagnetic centre, probably Ni(III). The hydrogenase was inhibited by heavy-metal salts, carbon monoxide and high ionic strength. However, it was resistant to inhibition by thiol-blocking and metal-complexing reagents. N-Bromosuccinimide totally inhibited the enzyme activity at low concentrations. The enzyme was stable to O2 over long periods and to high temperatures. It catalyses both H2-evolution and H2-uptake with a variety of artificial electron carriers. D. desulfuricans cytochrome C3, its natural electron carrier, had a high affinity for the enzyme (Km = 2 microns). Rate enhancement was observed when cytochrome C3 was added to Methyl Viologen in the H2-evolution assay. The pH optimum for H2-evolution was 6.5. | lld:pubmed |
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| pubmed-article:6303306 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6303306 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6303306 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6303306 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:6303306 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6303306 | pubmed:author | pubmed-author:RaoK KKK | lld:pubmed |
| pubmed-article:6303306 | pubmed:author | pubmed-author:CammackRR | lld:pubmed |
| pubmed-article:6303306 | pubmed:author | pubmed-author:HallD ODO | lld:pubmed |
| pubmed-article:6303306 | pubmed:author | pubmed-author:Le GallJJ | lld:pubmed |
| pubmed-article:6303306 | pubmed:author | pubmed-author:Lalla-Maharaj... | lld:pubmed |
| pubmed-article:6303306 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6303306 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6303306 | pubmed:volume | 209 | lld:pubmed |
| pubmed-article:6303306 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6303306 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6303306 | pubmed:pagination | 445-54 | lld:pubmed |
| pubmed-article:6303306 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:6303306 | pubmed:meshHeading | pubmed-meshheading:6303306-... | lld:pubmed |
| pubmed-article:6303306 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6303306 | pubmed:articleTitle | Purification and properties of the membrane-bound by hydrogenase from Desulfovibrio desulfuricans. | lld:pubmed |
| pubmed-article:6303306 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6303306 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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