Linked Life Data

1846226

Source:http://linkedlifedata.com/resource/pubmed/id/1846226

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6306
pubmed:dateCreated
1991-2-20
pubmed:abstractText
The role of copper in copper-containing amine oxidases has long been a source of debate and uncertainty. Numerous electron paramagnetic resonance (EPR) experiments, including rapid freeze-quench studies, have failed to detect changes in the copper oxidation state in the presence of substrate amines. One suggestion that copper reduction might occur, has never been confirmed. Copper amine oxidases contain another cofactor, recently identified as 6-hydroxydopa quinone (topa quinone), which is reduced by substrates. Copper has been implicated in the reoxidation of the substrate-reduced enzyme, but the failure to detect any copper redox change has led to proposals that Cu(II) acts as a Lewis acid, that it has an indirect role in catalysis, or that it serves a structural role. We present evidence for the generation of a Cu(I)-semiquinone state by substrate reduction of several amine oxidases under anaerobic conditions, and suggest that the Cu(I)-semiquinone may be the catalytic intermediate that reacts directly with oxygen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
349
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
262-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
A Cu(I)-semiquinone state in substrate-reduced amine oxidases.
pubmed:affiliation
Department of Chemistry, Amherst College, Massachusetts 01002.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't