| pubmed-article:12517128 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C0001026 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C0017963 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C1428910 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C0301630 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C1321758 | lld:lifeskim |
| pubmed-article:12517128 | lifeskim:mentions | umls-concept:C1611588 | lld:lifeskim |
| pubmed-article:12517128 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12517128 | pubmed:dateCreated | 2003-1-8 | lld:pubmed |
| pubmed-article:12517128 | pubmed:abstractText | Stopped-flow was used to evaluate the methylation and reduction kinetics of the isolated alpha subunit of acetyl-Coenzyme A synthase from Moorella thermoacetica. This catalytically active subunit contains a novel Ni-X-Fe4S4 cluster and a putative unidentified n = 2 redox site called D. The D-site must be reduced for a methyl group to transfer from a corrinoid-iron-sulfur protein, a key step in the catalytic synthesis of acetyl-CoA. The Fe4S4 component of this cluster is also redox active, raising the possibility that it is the D-site or a portion thereof. Results presented demonstrate that the D-site reduces far faster than the Fe4S4 component, effectively eliminating this possibility. Rather, this component may alter catalytically important properties of the Ni center. The D-site is reduced through a pathway that probably does not involve the Fe4S4 component of this active-site cluster. | lld:pubmed |
| pubmed-article:12517128 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12517128 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12517128 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12517128 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12517128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12517128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12517128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12517128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12517128 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12517128 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:12517128 | pubmed:issn | 0002-7863 | lld:pubmed |
| pubmed-article:12517128 | pubmed:author | pubmed-author:YangQingwuQ | lld:pubmed |
| pubmed-article:12517128 | pubmed:author | pubmed-author:LindahlPaul... | lld:pubmed |
| pubmed-article:12517128 | pubmed:author | pubmed-author:SewellChristo... | lld:pubmed |
| pubmed-article:12517128 | pubmed:author | pubmed-author:TanXiangshiX | lld:pubmed |
| pubmed-article:12517128 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12517128 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:12517128 | pubmed:volume | 125 | lld:pubmed |
| pubmed-article:12517128 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12517128 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12517128 | pubmed:pagination | 318-9 | lld:pubmed |
| pubmed-article:12517128 | pubmed:dateRevised | 2008-1-17 | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:meshHeading | pubmed-meshheading:12517128... | lld:pubmed |
| pubmed-article:12517128 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12517128 | pubmed:articleTitle | Reduction and methyl transfer kinetics of the alpha subunit from acetyl coenzyme a synthase. | lld:pubmed |
| pubmed-article:12517128 | pubmed:affiliation | Department of Chemistry, Texas A&M University, College Station 77843, USA. | lld:pubmed |
| pubmed-article:12517128 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12517128 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12517128 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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