Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1986-12-31
|
pubmed:abstractText |
The activation energy for the formation of the first red compound, ES, for cytochrome-c peroxidase (ferrocytochrome-c: hydrogen-peroxide oxidoreductase, EC 1.11.1.5) by i-propyl hydroperoxide and the rate constants for the formation of ES with various hydroperoxides have been determined. Multivariate data analysis by the partial least-squares model in latent variables has been used to compare the rate constants with the corresponding rate constants for the formation of compound I from lactoperoxidase and two isoenzymes of horseradish peroxidase. The results show that the rate of formation of ES from cytochrome-c peroxidase is highly correlated with the pKa of the hydroperoxides. The activation energy for the formation of ES with i-propyl hydroperoxide is close to the corresponding value for hydrogen peroxide.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
21
|
pubmed:volume |
874
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
160-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:3022815-Cytochrome-c Peroxidase,
pubmed-meshheading:3022815-Horseradish Peroxidase,
pubmed-meshheading:3022815-Kinetics,
pubmed-meshheading:3022815-Lactoperoxidase,
pubmed-meshheading:3022815-Peroxidases,
pubmed-meshheading:3022815-Protein Binding,
pubmed-meshheading:3022815-Saccharomyces cerevisiae,
pubmed-meshheading:3022815-Substrate Specificity
|
pubmed:year |
1986
|
pubmed:articleTitle |
The formation of ES of cytochrome-c peroxidase: a comparison with lactoperoxidase and horseradish peroxidase.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|