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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1990-11-9
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pubmed:abstractText |
The electron paramagnetic (EPR) properties of a transient species detected during a cytochrome P450 (P450)-mediated peroxidative reaction have been compared with those of peroxidases Compound I and model metalloporphyrins. The reaction which was studied with cholesterol-specific P450scc and (20R)-20-hydroperoxycholesterol, occurred without enzyme denaturation. The resulting transient species, which reached its maximum after 50 s reaction, was characterized by a one-line EPR spectrum, g = 2.0035, delta 1/2 = 1.08 mT. The decay of this radical was concomitant with the production of (20R)-20,21-dihydroxycholesterol. The reaction (almost 100% yield) conserved the stereo-specificity of the natural pathway. We suggest this intermediate is a candidate for the in vivo ultimate oxidant in the P450-mediated hydroxylation process. The comparison of the observed EPR spectrum with those of peroxidase Compound I and related synthetic models allows us to propose a FeIV porphyrin II cation radical structure for the intermediate.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/20-hydroperoxycholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Monoxide,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Side-Chain Cleavage...,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxycholesterols
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
198-201
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:2171430-Adrenal Cortex,
pubmed-meshheading:2171430-Animals,
pubmed-meshheading:2171430-Carbon Monoxide,
pubmed-meshheading:2171430-Cattle,
pubmed-meshheading:2171430-Cholesterol,
pubmed-meshheading:2171430-Cholesterol Side-Chain Cleavage Enzyme,
pubmed-meshheading:2171430-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:2171430-Free Radicals,
pubmed-meshheading:2171430-Hydroxycholesterols,
pubmed-meshheading:2171430-Hydroxylation,
pubmed-meshheading:2171430-Kinetics,
pubmed-meshheading:2171430-Oxidation-Reduction,
pubmed-meshheading:2171430-Protein Binding
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pubmed:year |
1990
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pubmed:articleTitle |
On the nature of the cytochrome P450scc "ultimate oxidant": characterization of a productive radical intermediate.
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pubmed:affiliation |
Institut National de la Santé et de la Recherche Médicale, Unité 128, Montpellier, France.
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pubmed:publicationType |
Journal Article
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