Linked Life Data

7692046

Source:http://linkedlifedata.com/resource/pubmed/id/7692046

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1993-10-29
pubmed:abstractText
Arginine is oxidized by a class of enzymes called the nitric oxide synthases (NOS) to generate citrulline and, presumably, nitric oxide (.NO). N-Hydroxylation of a guanidinium nitrogen of arginine to generate N-hydroxyarginine (NOHA) has been shown to be a step in the biosynthesis of .NO. In an effort to elucidate the mechanism by which further oxidation of NOHA occurs, the oxidation of a model N-hydroxyguanidine compound by several peracids was studied in depth. This oxidative chemistry is a possible model for the enzymatic process since the corresponding urea (or citrulline equivalent product) is obtained along with an oxidized nitrogen species. The oxidized nitrogen product was, however, not .NO but rather HNO. .NO generation in this chemical system and in the enzymatic process would require another one-electron oxidation. The mechanistic details of this are further discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2666-70
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Peracid oxidation of an N-hydroxyguanidine compound: a chemical model for the oxidation of N omega-hydroxyl-L-arginine by nitric oxide synthase.
pubmed:affiliation
Department of Pharmacology, UCLA School of Medicine 90024.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't