Linked Life Data

15643881

Source:http://linkedlifedata.com/resource/pubmed/id/15643881

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-1-12
pubmed:abstractText
The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty (Ty(met)) and its halide (F(-), Cl(-)) bound derivatives with a dissociation constant in the mM range. The Cu(2) bridging halide ion is not displaced upon the binding of pnp showing that the pnp does not occupy the Cu(2) bridging position. The binding of pnp to Ty(met) or Ty(met)Cl leads to localized changes in the type-3 (Cu-His(3))(2) coordination geometry reflecting a change in the coordination of a single His residue that, still, remains coordinated to Cu. The binding of pnp to Ty(met)Cl causes a decrease in the Cu(2) magnetic exchange parameter -2J from 200 cm(-)(1) in the absence to 150 +/- 10 cm(-)(1) in the presence of pnp. From the (1)H and (2)D NMR relaxation parameters of pnp bound to Ty(met), a structural model of pnp coordination to the Ty type-3 center could be derived. The model explains the absence of hydroxylase activity in the closely related type-3 copper protein catechol oxidase. The relevance of the experimental findings toward the Ty catalytic mechanism is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
567-75
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
pubmed:affiliation
Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't