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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1993-10-12
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pubmed:abstractText |
The heme domain of cellobiose oxidase (CBO) from Phanerochaete chrysosporium increases the rate of electron transfer to one-electron acceptors. This conclusion was drawn from comparisons of the rates of reduction of 3,5-t-butyl-o-benzoquinone, triiodide ion, cytochrome c and ferricyanide by intact CBO, FAD fragment and CBO with the heme inactivated by cyanide. The oxidation of cellobiose produced hydrogen peroxide, but the enzyme disturbs peroxidase-based assays by reduction of the product or by direct interaction with the peroxidase. CBO can also degrade hydrogen peroxide in the presence of cellobiose. The 1,2,4,5-tetramethoxybenzene cation radical was rapidly reduced by CBO.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
1144
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
184-90
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1993
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pubmed:articleTitle |
Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?
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pubmed:affiliation |
Department of Biochemistry, University of Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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