Linked Life Data

20615385

Source:http://linkedlifedata.com/resource/pubmed/id/20615385

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-8-31
pubmed:abstractText
Tris(p-carboxyltetrathiaaryl)methyl radicals (TAM*) are good EPR probes for measurement of dioxygen concentration in biological systems and for EPR imaging. It has been previously reported that these radicals are efficiently oxidized by superoxide, O2*(-), or alkylperoxyl radicals, ROO*, and by liver microsomes via an oxidative decarboxylation mechanism leading to the corresponding quinone-methides (QM). This article shows that peroxidases, such as horseradish peroxidase (HRP), lactoperoxidase (LPO) and prostaglandin synthase (PGHS), and other hemeproteins, such as methemoglobin (metHb), metmyoglobin (metMb) and catalase, also efficiently catalyze the oxidation of TAM* radicals to QM by H2O2 or alkylhydroperoxides. These reactions involve the intermediate formation of the corresponding cations TAM(+) that have also been cleanly generated by K2Ir(IV)Cl6 and characterized by UV-Visible spectroscopy and mass spectrometry, and through their reactions with ascorbate or H2O2. Labelling experiments on HRP-catalyzed oxidation of TAM* to QM using H2(18)O or (18)O2 in the presence of glucose and glucose oxidase (GOX) showed that the oxygen atom incorporated into QM came both from O2 and from H2O. Mechanisms for these reactions in agreement with those data were proposed. Oxidative decarboxylation of TAM* to QM is a new reaction catalyzed by peroxidases. Such reactions should be considered when using TAM* as EPR oximetry probes in vivo or in vitro in complex biological media.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1096-0384
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
502
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
74-80
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Oxidative decarboxylation of tris-(p-carboxyltetrathiaaryl)methyl radical EPR probes by peroxidases and related hemeproteins: intermediate formation and characterization of the corresponding cations.
pubmed:affiliation
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, UMR 8601 CNRS, Université Paris Descartes, 45 rue des Saints Pères, 75270 Paris Cedex 06, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't