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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1982-12-2
|
| pubmed:abstractText |
The mechanism of P-450 catalyzed reactions is discussed. They are shown not to be true peroxidase reactions. Liver microsome P-450 is capable of oxidizing such substrates as benzphenamine, amidopyrine and p-nitroanisole via molecular oxygen reduced on the cathode. The methods of stabilizing the enzymic system by means of immobilization of microsomes or isolated components are described. The possibility of coupling the enzymic and the electrochemical system is considered. The approaches to the modelling of the cytochrome P-450 catalytic activity with the aid of ferroporphyrine are proposed.
|
| pubmed:language |
rus
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0555-1099
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
18
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
481-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7122438-Catalysis,
pubmed-meshheading:7122438-Cytochrome P-450 Enzyme System,
pubmed-meshheading:7122438-Electrochemistry,
pubmed-meshheading:7122438-Electron Transport,
pubmed-meshheading:7122438-Fermentation,
pubmed-meshheading:7122438-Hydroxylation,
pubmed-meshheading:7122438-Metalloporphyrins,
pubmed-meshheading:7122438-Microsomes, Liver,
pubmed-meshheading:7122438-Oxidation-Reduction,
pubmed-meshheading:7122438-Peroxidases
|
| pubmed:articleTitle |
[Use of cytochrome P-450 and ferroporphyrin as catalyzers in hydroxylation reactions jointly with electrochemical systems].
|
| pubmed:publicationType |
Journal Article,
English Abstract
|