Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-6-19
pubmed:abstractText
A superfamily of mononuclear iron proteins, originally named desulfoferrodoxin and neelaredoxin, has been identified by in vivo and in vitro studies as scavengers of the superoxide anion radical. These proteins, whose genes are present in all the so-far known genomes from anaerobes and in the microaerophilic pathogen Treponema pallidum, show not only a considerable amino acid sequence identity but, most importantly, a common active iron site, Fe[His(4)CysGlu], in the oxidized state which loses the glutamate ligand in the reduced form. The experimental evidence for the activity of these proteins as superoxide dismutases or as donor:superoxide oxidoreductases is discussed in this Commentary, giving particular emphasis to the neelaredoxin from the hyperthermophilic archaeon Archaeoglobus fulgidus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0949-8257
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
668-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Superoxide scavenging by neelaredoxin: dismutation and reduction activities in anaerobes.
pubmed:affiliation
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780-156 Oeiras, Portugal.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't