Linked Life Data

10205052

Source:http://linkedlifedata.com/resource/pubmed/id/10205052

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5413
pubmed:dateCreated
1999-5-4
pubmed:databankReference
pubmed:abstractText
The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
284
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
473-6
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
A steric mechanism for inhibition of CO binding to heme proteins.
pubmed:affiliation
Max-Planck-Arbeitsgruppen für Strukturelle Molekularbiologie, Arbeitsgruppe Proteindynamik, Notkestrabetae 85, 22603 Hamburg, Germany.
pubmed:publicationType
Journal Article