Linked Life Data

16719449

Source:http://linkedlifedata.com/resource/pubmed/id/16719449

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2006-5-24
pubmed:abstractText
Oxygenation of a series of p-substituted phenols to the corresponding catechols (phenolase activity) by the (mu-eta2:eta2-peroxo)dicopper(II) species of Octopus hemocyanin has been directly examined for the first time by using a UV-vis spectroscopic method in a 0.5 M borate buffer solution containing 8 M urea under anaerobic conditions. Preliminary kinetic studies have indicated that the reaction involves an electrophilic aromatic substitution mechanism as in the case of phenolase reaction of tyrosinase. The oxygenation of phenols by hemocyanin also proceeded catalytically when the reaction was carried out under aerobic conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
128
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6788-9
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Significant enhancement of monooxygenase activity of oxygen carrier protein hemocyanin by urea.
pubmed:affiliation
Department of Chemistry, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't