Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-6-14
pubmed:abstractText
Oscillatory kinetics in the peroxidase-oxidase reaction catalyzed by structurally different peroxidases were investigated using NADH as a substrate. For horseradish peroxidase, lactoperoxidase, and soybean peroxidase the oscillatory waveforms of their dominating enzyme intermediates, ferric peroxidase and compound III, are similar. Coprinus peroxidase, on the other hand, has ferrous peroxidase and compound III as the dominating intermediates. The oscillatory waveform of its compound III differs from the waveforms of compound III of the three other peroxidases. Also, the phase plot of the signal for compound III versus the oxygen concentration for Coprinus peroxidase differs from the corresponding phase plots obtained using other peroxidases. A detailed model of the reaction mechanism is proposed, which is able to simulate these different kinds of behaviour. Substituting NADH with dihydroxyfumaric acid as a substrate, oscillations in the oxygen concentration were observed for about 1.5 h when a concentrated solution of this substrate was continuously fed to a solution containing horseradish peroxidase. This is the first demonstration of sustained oscillations with this substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
1289
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
377-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Kinetic studies of the oscillatory dynamics in the peroxidase-oxidase reaction catalyzed by four different peroxidases.
pubmed:affiliation
Institute of Biochemistry, Odense University, Odense, Denmark. valeur@sc2a.unige.ch
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't