Linked Life Data

17220900

Source:http://linkedlifedata.com/resource/pubmed/id/17220900

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-1-19
pubmed:databankReference
http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424980, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424981, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424982, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424983, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424984, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424985, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424986, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424987, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424988, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424989, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424990, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424991, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424992, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424993, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424994, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424995, http://linkedlifedata.com/resource/pubmed/xref/PubChem-Substance/17424996
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.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1552-4450
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-6
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3.
pubmed:affiliation
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural