| pubmed-article:21806784 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21806784 | lifeskim:mentions | umls-concept:C0521346 | lld:lifeskim |
| pubmed-article:21806784 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:21806784 | lifeskim:mentions | umls-concept:C0005104 | lld:lifeskim |
| pubmed-article:21806784 | lifeskim:mentions | umls-concept:C0016570 | lld:lifeskim |
| pubmed-article:21806784 | lifeskim:mentions | umls-concept:C0020275 | lld:lifeskim |
| pubmed-article:21806784 | lifeskim:mentions | umls-concept:C1151028 | lld:lifeskim |
| pubmed-article:21806784 | pubmed:dateCreated | 2011-8-25 | lld:pubmed |
| pubmed-article:21806784 | pubmed:abstractText | Escherichia coli synthesizes three membrane-bound molybdenum- and selenocysteine-containing formate dehydrogenases, as well as up to four membrane-bound [NiFe]-hydrogenases. Two of the formate dehydrogenases (Fdh-N and Fdh-O) and two of the hydrogenases (Hyd-1 and Hyd-2) have their respective catalytic subunits located in the periplasm and these enzymes have been shown previously to oxidize formate and hydrogen, respectively, and thus function in energy metabolism. Mutants unable to synthesize the [NiFe]-hydrogenases retain a H?: benzyl viologen oxidoreductase activity. The aim of this study was to identify the enzyme or enzymes responsible for this activity. | lld:pubmed |
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| pubmed-article:21806784 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21806784 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21806784 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21806784 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21806784 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21806784 | pubmed:issn | 1471-2180 | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:IhlingChristi... | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:SawersGaryG | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:TrchounianArm... | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:SinzAndreaA | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:SobohBasemB | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:TrchounianKar... | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:KuhnsMartinM | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:PinskeConstan... | lld:pubmed |
| pubmed-article:21806784 | pubmed:author | pubmed-author:WaclawekMandy... | lld:pubmed |
| pubmed-article:21806784 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21806784 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:21806784 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21806784 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21806784 | pubmed:pagination | 173 | lld:pubmed |
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| pubmed-article:21806784 | pubmed:meshHeading | pubmed-meshheading:21806784... | lld:pubmed |
| pubmed-article:21806784 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21806784 | pubmed:articleTitle | The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia coli have hydrogen: benzyl viologen oxidoreductase activity. | lld:pubmed |
| pubmed-article:21806784 | pubmed:affiliation | Institute for Microbiology, Martin-Luther University Halle-Wittenberg, Kurt-Mothes-Str, 3, 06120 Halle (Saale), Germany. | lld:pubmed |
| pubmed-article:21806784 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21806784 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
