| pubmed-article:17220900 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17220900 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:17220900 | lifeskim:mentions | umls-concept:C0051179 | lld:lifeskim |
| pubmed-article:17220900 | lifeskim:mentions | umls-concept:C0175961 | lld:lifeskim |
| pubmed-article:17220900 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17220900 | pubmed:dateCreated | 2007-1-19 | lld:pubmed |
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| pubmed-article:17220900 | pubmed:abstractText | Enzymatic incorporation of a halogen atom is a common feature in the biosyntheses of more than 4,500 natural products. Halogenation of unactivated carbon centers in the biosyntheses of several compounds of nonribosomal peptide origin is carried out by a class of mononuclear nonheme iron enzymes that require alpha-ketoglutarate (alphaKG, 1), chloride and oxygen. To investigate the ability of these enzymes to functionalize unactivated methyl groups, we characterized the chlorination of the gamma-methyl substituent of L-2-aminobutyric acid (L-Aba, 2) attached to the carrier protein CytC2 by iron halogenase (CytC3) from soil Streptomyces sp. We identified an intermediate state comprising two high-spin Fe(IV) complexes in rapid equilibrium. At least one of the Fe(IV) complexes abstracts hydrogen from the substrate. The demonstration that chlorination proceeds through an Fe(IV) intermediate that cleaves a C-H bond reveals the mechanistic similarity of aliphatic halogenases to the iron- and alphaKG-dependent hydroxylases. | lld:pubmed |
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| pubmed-article:17220900 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17220900 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17220900 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17220900 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17220900 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17220900 | pubmed:issn | 1552-4450 | lld:pubmed |
| pubmed-article:17220900 | pubmed:author | pubmed-author:WalshChristop... | lld:pubmed |
| pubmed-article:17220900 | pubmed:author | pubmed-author:KrebsCarstenC | lld:pubmed |
| pubmed-article:17220900 | pubmed:author | pubmed-author:BollingerJ... | lld:pubmed |
| pubmed-article:17220900 | pubmed:author | pubmed-author:BarrEric WEW | lld:pubmed |
| pubmed-article:17220900 | pubmed:author | pubmed-author:Galoni?Danica... | lld:pubmed |
| pubmed-article:17220900 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17220900 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:17220900 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17220900 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17220900 | pubmed:pagination | 113-6 | lld:pubmed |
| pubmed-article:17220900 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
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| pubmed-article:17220900 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17220900 | pubmed:articleTitle | Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3. | lld:pubmed |
| pubmed-article:17220900 | pubmed:affiliation | Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:17220900 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17220900 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17220900 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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