Linked Life Data

12940720

Source:http://linkedlifedata.com/resource/pubmed/id/12940720

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
2003-8-27
pubmed:abstractText
Nitrite ion is found to catalyze the NO reduction of met-hemoglobin and met-myoglobin in pH 7.0 buffered aqueous solution. The catalysis rate constants for these ferriheme proteins and for two water-soluble ferriheme model systems follow the same order as do the FeIII/II reduction potentials of the ferric nitrosyl complexes. This is consistent with a proposed mechanism occurring via outer sphere reduction of the FeIII(NO) center by NO2- to give the FeII(NO) product plus NO2. Although the first step is thermodynamically uphill, the NO2 generated would be rapidly trapped by excess NO to form N2O3, which would hydrolyze. We speculate that, if formed in the proximity of the protein, the strong nitrosating agent N2O3 could also result in protein modifications.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10510-1
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Nitrite catalyzes ferriheme protein reductive nitrosylation.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.