| pubmed-article:18459773 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C0017963 | lld:lifeskim |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C1412810 | lld:lifeskim |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C1417607 | lld:lifeskim |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C1423773 | lld:lifeskim |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C0108413 | lld:lifeskim |
| pubmed-article:18459773 | lifeskim:mentions | umls-concept:C1321758 | lld:lifeskim |
| pubmed-article:18459773 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:18459773 | pubmed:dateCreated | 2008-5-21 | lld:pubmed |
| pubmed-article:18459773 | pubmed:abstractText | The active site A-cluster in the alpha subunit of the title enzyme consists of an Fe4S4 cluster coordinated to a [Nip Nid] subcomponent. The cluster must be activated for catalysis using low-potential reductants such as Ti(III) citrate. Relative to the inactive {[Fe4S4]2+ Nip2+ Nid2+} state, the activated state appears to be 2-electrons more reduced, but the location of these electrons within the A-cluster is uncertain, with {[Fe4S4]2+ Nip0 Nid2+} and {[Fe4S4]1+ Nip1+ Nid2+} configurations proposed. Recombinant apo-alpha subunits oligomerize after activation with NiCl2. The dimer fraction, upon reduction with excess Ti(III)citrate, exhibited Mössbauer spectra consisting of two quadrupole doublets representing 51% and 21% of the Fe, with parameters indicating [Fe4S4]1+ states. Spectra recorded in strong magnetic fields were typical of diamagnetic systems, indicating an exchange-coupled S = 0 {[Fe4S4]1+ Nip1+} state. Additional treatment with CO altered the doublet Mössbauer parameters, suggesting an interaction with CO, but maintaining the cluster in the {[Fe4S4]1+ Nip1+} state. Reduction with substoichiometric equivalents of Ti(III) citrate afforded an EPR signal typical of Ni1+ ions, with g parallel = 2.10 and g perpendicular = 2.02. Addition of more Ti caused the signal intensity to decline, suggesting that it arises from the semireduced {[Fe4S4]2+ Nip1+} state. | lld:pubmed |
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| pubmed-article:18459773 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18459773 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18459773 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18459773 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18459773 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18459773 | pubmed:month | May | lld:pubmed |
| pubmed-article:18459773 | pubmed:issn | 1520-5126 | lld:pubmed |
| pubmed-article:18459773 | pubmed:author | pubmed-author:MünckEckardE | lld:pubmed |
| pubmed-article:18459773 | pubmed:author | pubmed-author:LindahlPaul... | lld:pubmed |
| pubmed-article:18459773 | pubmed:author | pubmed-author:StubnaAudriaA | lld:pubmed |
| pubmed-article:18459773 | pubmed:author | pubmed-author:TanXiangshiX | lld:pubmed |
| pubmed-article:18459773 | pubmed:author | pubmed-author:MartinhoMarlè... | lld:pubmed |
| pubmed-article:18459773 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18459773 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:18459773 | pubmed:volume | 130 | lld:pubmed |
| pubmed-article:18459773 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18459773 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18459773 | pubmed:pagination | 6712-3 | lld:pubmed |
| pubmed-article:18459773 | pubmed:dateRevised | 2011-4-28 | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:meshHeading | pubmed-meshheading:18459773... | lld:pubmed |
| pubmed-article:18459773 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18459773 | pubmed:articleTitle | Mossbauer evidence for an exchange-coupled {[Fe4S4]1+ Nip1+} A-cluster in isolated alpha subunits of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase. | lld:pubmed |
| pubmed-article:18459773 | pubmed:affiliation | Department of Chemistry and Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, USA. | lld:pubmed |
| pubmed-article:18459773 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18459773 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18459773 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18459773 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18459773 | lld:pubmed |
