| pubmed-article:18838684 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18838684 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:18838684 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:18838684 | lifeskim:mentions | umls-concept:C0068811 | lld:lifeskim |
| pubmed-article:18838684 | pubmed:issue | 41 | lld:pubmed |
| pubmed-article:18838684 | pubmed:dateCreated | 2008-10-16 | lld:pubmed |
| pubmed-article:18838684 | pubmed:abstractText | A functional heme/nonheme nitric oxide reductase (NOR) model is presented. The fully reduced diiron compound reacts with two equivalents of NO leading to the formation of one equivalent of N(2)O and the bis-ferric product. NO binds to both heme Fe and nonheme Fe complexes forming individual ferrous nitrosyl species. The mixed-valence species with an oxidized heme and a reduced nonheme Fe(B) does not show NO reduction activity. These results are consistent with a so-called "trans" mechanism for the reduction of NO by bacterial NOR. | lld:pubmed |
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| pubmed-article:18838684 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18838684 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18838684 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18838684 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:18838684 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:18838684 | pubmed:author | pubmed-author:YangYingY | lld:pubmed |
| pubmed-article:18838684 | pubmed:author | pubmed-author:CollmanJames... | lld:pubmed |
| pubmed-article:18838684 | pubmed:author | pubmed-author:SolomonEdward... | lld:pubmed |
| pubmed-article:18838684 | pubmed:author | pubmed-author:OhtaTakehiroT | lld:pubmed |
| pubmed-article:18838684 | pubmed:author | pubmed-author:DeyAbhishekA | lld:pubmed |
| pubmed-article:18838684 | pubmed:author | pubmed-author:GhoshSomdatta... | lld:pubmed |
| pubmed-article:18838684 | pubmed:author | pubmed-author:DecréauRichar... | lld:pubmed |
| pubmed-article:18838684 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18838684 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:18838684 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:18838684 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18838684 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18838684 | pubmed:pagination | 15660-5 | lld:pubmed |
| pubmed-article:18838684 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:18838684 | pubmed:meshHeading | pubmed-meshheading:18838684... | lld:pubmed |
| pubmed-article:18838684 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18838684 | pubmed:articleTitle | A functional nitric oxide reductase model. | lld:pubmed |
| pubmed-article:18838684 | pubmed:affiliation | Department of Chemistry, Stanford University, Stanford, CA 94305, USA. jpc@stanford.edu | lld:pubmed |
| pubmed-article:18838684 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18838684 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18838684 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18838684 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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