Linked Life Data

8886285

Source:http://linkedlifedata.com/resource/pubmed/id/8886285

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-4
pubmed:abstractText
A simple model, 4-tert-butyl-1,2-benzoquinone, was chosen to study the hydroxylation step of the tyrosine-derived Dopaquinone residue at the active site of copper amine oxidases in the self-catalytic generation of the Topaquinone cofactor. This hydroxylation step was studied both in the presence and absence of free copper(II), and was found to be dependent on pH value but not on the presence of metal ions. It is therefore proposed that, hydroxide ion and not water should be the true reactive species in this key biosynthetic step of the Topaquinone cofactor, and that the active site Cu2+ is implied, at this point of cofactor biosynthesis, in the quinonisation of Topa rather than in the hydroxylation of Dopaquinone.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
189-97
pubmed:dateRevised
2001-11-2
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Dopaquinone hydroxylation through topaquinone cofactor in copper amine oxidases: a simplified chemical model.
pubmed:affiliation
Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Università di Roma Tor Vergata, Italy.
pubmed:publicationType
Journal Article