Linked Life Data

10956005

Source:http://linkedlifedata.com/resource/pubmed/id/10956005

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2000-9-12
pubmed:abstractText
The iron ligand CO stretch vibration mode of the inducible nitric oxide synthase oxygenase domain (iNOSox) has been studied from 20 to 298 K. iNOSox in the absence of arginine reveals a temperature-dependent equilibrium of two major conformational substates with CO stretch bands centered at about 1945 and 1954 cm(-)(1). This behavior is not qualitatively changed when tetrahydrobiopterin (H(4)B) is bound. Arginine binding changes significantly the spectrum by formation of a sharp CO stretch mode band at about 1905 cm(-)(1) and indicates the formation of a hydrogen bond to the CO ligand. For temperatures lower than 250 K, the stretch vibration frequency decreases almost linearly with decreasing temperature and indicates that the coupling between the CO ligand and the arginine/protein in the active site via the hydrogen bond is very strong. Flashphotolysis of the CO ligand carried out at 25 K revealed the CO stretch mode of the photodissociated CO ligand trapped in the heme pocket. There is a negative linear relation between the stretch vibration frequencies of the photodissociated and the iron-bound CO indicating that the photodissociated ligand stays near the heme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10163-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
FT-Infrared spectroscopic studies of the iron ligand CO stretch mode of iNOS oxygenase domain: effect of arginine and tetrahydrobiopterin.
pubmed:affiliation
Max-Delbrück-Center for Molecular Medicine, Robert-Rössle-Strasse Berlin, Germany. cjung@mdc-berlin.de
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't