Linked Life Data

2145978

Source:http://linkedlifedata.com/resource/pubmed/id/2145978

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-12-4
pubmed:abstractText
The equilibrium and the kinetics of the reaction between Neurospora crassa tyrosinase and cyanide have been studied. Cyanide reacts with the binuclear copper active site of the protein competitively with respect to dioxygen and displaces the metal ions. This process occurs stepwise and involves transient intermediates containing mononuclear Cu(I) sites. The reaction mechanism proved to be the same as described earlier for molluscan and arthropodan hemocyanins, which share with tyrosinase the same copper active site organization, but perform different physiological functions. A comparison of the kinetic parameters between the different proteins shows that the tyrosinase copper active site has a greater accessibility than that of hemocyanin. The relevance of these data in terms of structure-function relationship and evolution of the binuclear copper proteins is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
1040
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
365-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The reaction of CN- with the binuclear copper site of Neurospora tyrosinase: its relevance for a comparison between tyrosinase and hemocyanin active sites.
pubmed:affiliation
Department of Biology, University of Padova, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't