| pubmed-article:1662489 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1662489 | lifeskim:mentions | umls-concept:C0995408 | lld:lifeskim |
| pubmed-article:1662489 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1662489 | lifeskim:mentions | umls-concept:C0001988 | lld:lifeskim |
| pubmed-article:1662489 | lifeskim:mentions | umls-concept:C0037812 | lld:lifeskim |
| pubmed-article:1662489 | lifeskim:mentions | umls-concept:C1533716 | lld:lifeskim |
| pubmed-article:1662489 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
| pubmed-article:1662489 | pubmed:dateCreated | 1992-2-11 | lld:pubmed |
| pubmed-article:1662489 | pubmed:abstractText | E.p.r. spectra of reduced iron-sulphur centres of the aldehyde oxidoreductase (iron-molybdenum protein) of Desulfovibrio gigas were recorded at X-band and Q-band frequencies and simulated. Results are consistent with the view that only two types of [2Fe-2S] clusters are present, as in eukaryotic molybdenum-containing hydroxylases. The data indicate the Fe/SI centre to be very similar, and the Fe/SII centre somewhat similar, to these centres in the eukaryotic enzymes. | lld:pubmed |
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| pubmed-article:1662489 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1662489 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1662489 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1662489 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1662489 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1662489 | pubmed:author | pubmed-author:BrayR CRC | lld:pubmed |
| pubmed-article:1662489 | pubmed:author | pubmed-author:Le GallJJ | lld:pubmed |
| pubmed-article:1662489 | pubmed:author | pubmed-author:MouraJ JJJ | lld:pubmed |
| pubmed-article:1662489 | pubmed:author | pubmed-author:BarataB ABA | lld:pubmed |
| pubmed-article:1662489 | pubmed:author | pubmed-author:TurnerN ANA | lld:pubmed |
| pubmed-article:1662489 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1662489 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1662489 | pubmed:volume | 280 ( Pt 3) | lld:pubmed |
| pubmed-article:1662489 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1662489 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1662489 | pubmed:pagination | 817-20 | lld:pubmed |
| pubmed-article:1662489 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:1662489 | pubmed:meshHeading | pubmed-meshheading:1662489-... | lld:pubmed |
| pubmed-article:1662489 | pubmed:meshHeading | pubmed-meshheading:1662489-... | lld:pubmed |
| pubmed-article:1662489 | pubmed:meshHeading | pubmed-meshheading:1662489-... | lld:pubmed |
| pubmed-article:1662489 | pubmed:meshHeading | pubmed-meshheading:1662489-... | lld:pubmed |
| pubmed-article:1662489 | pubmed:meshHeading | pubmed-meshheading:1662489-... | lld:pubmed |
| pubmed-article:1662489 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1662489 | pubmed:articleTitle | Information from e.p.r. spectroscopy on the iron-sulphur centres of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas. | lld:pubmed |
| pubmed-article:1662489 | pubmed:affiliation | School of Biological Sciences, University of Sussex, Brighton, U.K. | lld:pubmed |
| pubmed-article:1662489 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1662489 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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