| pubmed-article:9461283 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9461283 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:9461283 | lifeskim:mentions | umls-concept:C0524465 | lld:lifeskim |
| pubmed-article:9461283 | lifeskim:mentions | umls-concept:C0302583 | lld:lifeskim |
| pubmed-article:9461283 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9461283 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9461283 | lifeskim:mentions | umls-concept:C1513475 | lld:lifeskim |
| pubmed-article:9461283 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9461283 | pubmed:dateCreated | 1998-2-27 | lld:pubmed |
| pubmed-article:9461283 | pubmed:abstractText | A 2-His-1-carboxylate facial triad is a common feature of the active sites in a number of mononuclear non-heme iron(II) enzymes. This structural motif was established crystallographically for five different classes of enzymes and inferred from sequence similarity for two other classes. The 2-His-1-carboxylate facial triad anchors the iron in the active site and at the same time maintains three additional cis-oriented sites. These sites can be used to bind other endogenous ligands or exogenous ligands such as substrate and/or O2, giving the metal center great flexibility to use different mechanistic strategies to perform a variety of chemical transformations. | lld:pubmed |
| pubmed-article:9461283 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9461283 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461283 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9461283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9461283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461283 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9461283 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9461283 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:9461283 | pubmed:author | pubmed-author:QueLLJr | lld:pubmed |
| pubmed-article:9461283 | pubmed:author | pubmed-author:HeggE LEL | lld:pubmed |
| pubmed-article:9461283 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9461283 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9461283 | pubmed:volume | 250 | lld:pubmed |
| pubmed-article:9461283 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9461283 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9461283 | pubmed:pagination | 625-9 | lld:pubmed |
| pubmed-article:9461283 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:meshHeading | pubmed-meshheading:9461283-... | lld:pubmed |
| pubmed-article:9461283 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9461283 | pubmed:articleTitle | The 2-His-1-carboxylate facial triad--an emerging structural motif in mononuclear non-heme iron(II) enzymes. | lld:pubmed |
| pubmed-article:9461283 | pubmed:affiliation | Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis 55455, USA. | lld:pubmed |
| pubmed-article:9461283 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9461283 | pubmed:publicationType | Review | lld:pubmed |
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