Linked Life Data

7918479

Source:http://linkedlifedata.com/resource/pubmed/id/7918479

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
1994-11-22
pubmed:abstractText
X-ray absorption spectroscopy has been used to characterize the local structural environment of the Cu ion in the reductively inactivated, oxidatively activated, and active+substrate oxidation state derivatives of galactose oxidase. In all three cases, the local environment of the Cu is best modeled by a single shell of low-Z (N or O) scatterers. This is generally consistent with the structure determined crystallographically, although the EXAFS bond lengths are slightly, but significantly, shorter than those found crystallographically. The best-fit average bond lengths are 1.97, 1.95, and 1.98 A for inactive, active, and active+substrate, respectively. The CuII ion in the active and inactive derivatives has an apparent coordination number of 4, consistent with the equatorial ligation seen crystallographically. The CuI ion in the reduced+substrate derivative appears to have either a lower coordination number or a significantly more distorted local environment. The observed CuI-(N/O) bond length favors a model where the Cu become 3-coordinate in the substrate-reduced complex.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12553-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Structural characterization of the copper site in galactose oxidase using X-ray absorption spectroscopy.
pubmed:affiliation
Department of Chemistry, University of Michigan, Ann Arbor 48109-1055.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.