Linked Life Data

9345311

Source:http://linkedlifedata.com/resource/pubmed/id/9345311

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-11-24
pubmed:abstractText
Kinetic studies of soluble guanylate cyclase complexed with nitric oxide prove that NO dissociation in the presence of the substrate GTP and Mg2+ is as much as 50 times faster than in their absence. In the presence of those two reagents the dissociation rate constant is k(obs) = 0.04 +/- 0.01 s-1 at 20 degrees C, which is by far the fastest NO dissociation rate constant ever reported for a ferrous heme protein. Extrapolated to 37 degrees C, this corresponds to a half life of about 5 s for NO dissociation from soluble guanylate cyclase at physiological conditions, which is presumably fast enough to account for deactivation of the enzyme in biological systems. Dissociation rate constants are also reported for a variety of other reagent conditions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
239
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
284-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Dissociation of nitric oxide from soluble guanylate cyclase.
pubmed:affiliation
Department of Chemistry, University of California at San Diego, La Jolla 92093-0652, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.