Linked Life Data

10093938

Source:http://linkedlifedata.com/resource/pubmed/id/10093938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-5-19
pubmed:abstractText
The spectroscopic (UV-visible, IR, RR, MCD, Mössbauer, EPR), crystallographic, kinetic, and redox investigations that have been carried out on model hemes, hemoglobin, myoglobin, cytochrome a3 of cytochrome oxidase, horseradish peroxidase, prostaglandin H synthase, cytochromes P450, chloroperoxidase, and so forth have shown us the unique properties of heme-NO centers, as summarized above. However, in none of these cases is the Fe(III)NO complex of any known physiological importance. The nitrophorins of R. prolixus [59] (and Cimex lectularius [80]) are thus far unique in this respect. It is likely that further investigations of the roles of NO in biological systems will discover additional interesting involvements of heme proteins in these roles.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0161-5149
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
621-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Novel nitric oxide-liberating heme proteins from the saliva of bloodsucking insects.
pubmed:affiliation
Department of Chemistry, University of Arizona, Tucson 85721, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't