Source:http://linkedlifedata.com/resource/pubmed/id/10907744
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2000-10-3
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pubmed:abstractText |
Steady-state and single-turnover kinetics for the oxidation of the N-substituted phenothiazines (PTs) and phenoxazines (POs) catalyzed by fungal Coprinus cinereus peroxidase and Polyporus pinsitus laccase were investigated at pH 4-10. In the case of peroxidase, an apparent bimolecular rate constant (expressed as k(cat)/K(m)) varied from 1 x10(7)M(-1)s(-1) to 2.6 x 108 M(-1)s(-1) at pH 7.0. The constants for PO oxidation were higher in comparison to PT. pH dependence revealed two or three ionizable groups with pKa values of 4.9-5.7 and 7.7-9.7 that significantly affected the activity of peroxidase. Single-turnover experiments showed that the limiting step of PT oxidation was reduction of compound II and second-order rate constants were obtained which were consistent with the constants at steady-state conditions. Laccase-catalyzed PT and PO oxidation rates were lower; apparent bimolecular rate constants varied from 1.8x 10(5) M(-1) s(-1) to 2.0 x 10(7) M(-1) s(-1) at pH 5.3. PO constants were higher in comparison to PT, as was the case with peroxidase. The dependence of the apparent bimolecular constants of compound II or copper type 1 reduction, in the case of peroxidase or laccase, respectively, was analyzed in the framework of the Marcus outer-sphere electron-transfer theory. Peroxidase-catalyzed reactions with PT, as well as PO, fitted the same hyperbolic dependence with a maximal oxidation rate of 1.6 x 10(8)M(-1)s(-1) and a reorganization energy of 0.30 eV. The respective parameters for laccase were 5.0 x 10(7) M(-1) s(-1) and 0.29 eV.
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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/Antiprotozoal Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Laccase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxazines,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Phenothiazines,
http://linkedlifedata.com/resource/pubmed/chemical/phenothiazine,
http://linkedlifedata.com/resource/pubmed/chemical/phenoxazine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0949-8257
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
333-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10907744-Antiprotozoal Agents,
pubmed-meshheading:10907744-Coprinus,
pubmed-meshheading:10907744-Hydrogen-Ion Concentration,
pubmed-meshheading:10907744-Kinetics,
pubmed-meshheading:10907744-Laccase,
pubmed-meshheading:10907744-Oxazines,
pubmed-meshheading:10907744-Oxidation-Reduction,
pubmed-meshheading:10907744-Oxidoreductases,
pubmed-meshheading:10907744-Peroxidase,
pubmed-meshheading:10907744-Phenothiazines,
pubmed-meshheading:10907744-Polyporaceae,
pubmed-meshheading:10907744-Substrate Specificity,
pubmed-meshheading:10907744-Thermodynamics
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pubmed:year |
2000
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pubmed:articleTitle |
Kinetics and thermodynamics of peroxidase- and laccase-catalyzed oxidation of N-substituted phenothiazines and phenoxazines.
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pubmed:affiliation |
Institute of Biochemistry, Vilnius, Lithuania. jkulys@bchi.lt
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pubmed:publicationType |
Journal Article
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