Linked Life Data

21194610

Source:http://linkedlifedata.com/resource/pubmed/id/21194610

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-1-3
pubmed:abstractText
Since its discovery, nitric oxide synthase (NOS), the enzyme responsible for NO biosynthesis in mammals, has been the subject of extensive investigations regarding its catalytic and molecular mechanisms. These studies reveal the high degree of sophistication of NOS functioning and regulation. However, the precise description of the NOS molecular mechanism and in particular of the oxygen activation chemistry is still lacking. The reaction intermediates implicated in NOS catalysis continue to elude identification and the current working paradigm is increasingly contested. Consequently, the last three years has seen the emergence of several competing models. All these models propose the same global reaction scheme consisting of two successive oxidation reactions but they diverge in the details of their reaction sequence. The major discrepancies concern the number, source and characteristics of proton and electron transfer processes. As a result each model proposes distinct reaction pathways with different implied oxidative species. This review aims to examine the different experimental evidence concerning NOS proton and electron transfer events and the role played by the substrates and cofactors in these processes. The resulting discussion should provide a comparative picture of all potential models for the NOS molecular mechanism.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1873-3344
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
105
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
127-41
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
The molecular mechanism of mammalian NO-synthases: a story of electrons and protons.
pubmed:affiliation
iBiTec-S; LSOD, C. E. A. Saclay; 91191 Gif-sur-Yvette Cedex, France. jerome.santolini@cea.fr
pubmed:publicationType
Journal Article, Review