Linked Life Data

17521158

Source:http://linkedlifedata.com/resource/pubmed/id/17521158

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2007-7-20
pubmed:abstractText
One of the common biochemical pathways of binding and activation of dioxygen involves non-heme iron centers. The enzyme cycles usually start with an iron(II) or diiron(II) state and traverse via several intermediates (detected or postulated) such as (di)iron(III)-superoxo, (di)iron(III)-(hydro)peroxo, iron(III)iron(IV)-oxo, and (di)iron(IV)-oxo species, some of which are responsible for substrate oxidation. In this Account, we present results of kinetic and mechanistic studies of dioxygen binding and activation reactions of model inorganic iron compounds. The number of iron centers, their coordination number, and the steric and electronic properties of the ligands were varied in several series of well-characterized complexes that provided reactive manifolds modeling the function of native non-heme iron enzymes. Time-resolved cryogenic stopped-flow spectrophotometry permitted the identification of kinetically competent intermediates in these systems. Inner-sphere mechanisms dominated the chemistry of dioxygen binding, intermediate transformations, and substrate oxidation as most of these processes were controlled by the rates of ligand substitution at the iron centers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0001-4842
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
510-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Dioxygen activation at non-heme iron: insights from rapid kinetic studies.
pubmed:affiliation
Department of Chemistry, Tufts University, Medford, Massachusetts 02155, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review