Linked Life Data

1595127

Source:http://linkedlifedata.com/resource/pubmed/id/1595127

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1992-7-2
pubmed:abstractText
Sequence analyses of the Streptococcus faecalis NADH peroxidase and the flavoprotein component of the Salmonella typhimurium alkyl hydroperoxide reductase indicate clear evolutionary links with members of the flavoprotein disulfide reductase family. However, chemical and spectroscopic evidence demonstrate that the non-flavin redox center in NADH peroxidase is an unusual stabilized cysteine-sulfenic acid (Cys-SOH) derivative, and not a cystine disulfide as found in the disulfide reductases. This redox-active element, when appropriately stabilized by the respective protein environment, appears to play key roles in both the catalytic and regulatory aspects of the bacterial response to oxidative stress.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0968-0004
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response.
pubmed:affiliation
Department of Biochemistry, Wake Forest University Medical Center, Winston-Salem, NC 27157-1016.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't