| pubmed-article:10777518 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0038739 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0302583 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C1704332 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0013845 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C0701942 | lld:lifeskim |
| pubmed-article:10777518 | lifeskim:mentions | umls-concept:C1449016 | lld:lifeskim |
| pubmed-article:10777518 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:10777518 | pubmed:dateCreated | 2000-6-2 | lld:pubmed |
| pubmed-article:10777518 | pubmed:abstractText | We report an EPR study of the iron-sulfur enzyme, anaerobic ribonucleotide reductase activase from Lactococcus lactis. The activase (nrdG gene) together with S-adenosyl-L-methionine (AdoMet) give rise to a glycyl radical in the NrdD component. A semi-reduced [4Fe-4S](+) cluster with an axially symmetric EPR signal was produced upon photochemical reduction of the activase. Air exposure of the reduced enzyme gave a [3Fe-4S](+) cluster. The Fe(3)S(4) cluster was convertible to the EPR-active [4Fe-4S](+) cluster by renewed treatment with reducing agents, demonstrating a reversible [3Fe-4S](+)- to-[4Fe-4S](+) cluster conversion without exogenous addition of iron or sulfide. Anaerobic reduction of the activase by a moderate concentration of dithionite also resulted in a semi-reduced [4Fe-4S](+) cluster. Prolonged reduction gave an EPR-silent fully reduced state, which was enzymatically inactive. Both reduced states gave the [3Fe-4S](+) EPR signal after air exposure. The iron-sulfur cluster interconversion was also studied in the presence of AdoMet. The EPR signal of semi-reduced activase-AdoMet had rhombic symmetry and was independent of which reductant was applied, whereas the EPR signal of the [3Fe-4S](+) cluster after air exposure was unchanged. The results indicate that an AdoMet-mediated [4Fe-4S](+) center is the native active species that induces the formation of a glycyl radical in the NrdD component. | lld:pubmed |
| pubmed-article:10777518 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10777518 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10777518 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10777518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10777518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10777518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10777518 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10777518 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10777518 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10777518 | pubmed:author | pubmed-author:LipJJ | lld:pubmed |
| pubmed-article:10777518 | pubmed:author | pubmed-author:GräslundAA | lld:pubmed |
| pubmed-article:10777518 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10777518 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:10777518 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10777518 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10777518 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10777518 | pubmed:pagination | 12367-73 | lld:pubmed |
| pubmed-article:10777518 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10777518 | pubmed:meshHeading | pubmed-meshheading:10777518... | lld:pubmed |
| pubmed-article:10777518 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10777518 | pubmed:articleTitle | Electron paramagnetic resonance evidence for a novel interconversion of [3Fe-4S](+) and [4Fe-4S](+) clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activase in vitro. | lld:pubmed |
| pubmed-article:10777518 | pubmed:affiliation | Department of Biophysics, Arrhenius Laboratories, Stockholm University, S-106 91 Stockholm, Sweden. | lld:pubmed |
| pubmed-article:10777518 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10777518 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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