Linked Life Data

9667933

Source:http://linkedlifedata.com/resource/pubmed/id/9667933

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-9-11
pubmed:abstractText
Several major advances in our understanding of the structure, function and properties of biological iron-sulfur clusters have occurred in the past year. These include a new structural type of cluster in the inappropriately named prismane protein, the establishment of redox-mediated [Fe2S2]2+ <--> [Fe4S4]2+ cluster conversions, and the characterization of valence-delocalized [Fe2S2]+ and all ferrous clusters with [Fe2S2]0, [Fe3S4]2- and [Fe4S4]0 cores. The emergence of novel types of redox, regulatory and enzymatic roles have also raised the possibility of iron-sulfur clusters mediating two electron redox processes, coupling proton and electron transfer, and catalyzing disulfide reduction and reductive cleavage of S-adenosylmethionine via sulfur-based cluster chemistry.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1367-5931
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-81
pubmed:dateRevised
2009-8-25
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Iron-sulfur proteins: new roles for old clusters.
pubmed:affiliation
Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA. johnson@sunchem.chem.uga.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review