Linked Life Data

14871067

Source:http://linkedlifedata.com/resource/pubmed/id/14871067

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-2-11
pubmed:abstractText
Ultrafast spectroscopic measurements are used to determine the kinetics of homolysis and recombination for adenosylcobalamin bound in the active site of glutamate mutase. These are the first such measurements on an adenosylcobalamin-dependent enzyme. A short-lived intermediate is formed prior to formation of the cob(II)alamin radical. This intermediate was not observed upon photolysis of adenosylcobalamin in free solution. The intrinsic rate constant for geminate recombination for adenosylcobalamin bound to glutamate mutase is 1.08 +/- 0.10 ns-1, only 16% smaller than the rate constant measured in free solution, 1.39 +/- 0.06 ns-1, suggesting the protein does not greatly perturb the stability of the cobalt-carbon bond upon binding the coenzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1598-9
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Photolysis and recombination of adenosylcobalamin bound to glutamate mutase.
pubmed:affiliation
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA. rsension@umich.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.