Linked Life Data

16218868

Source:http://linkedlifedata.com/resource/pubmed/id/16218868

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2005-10-12
pubmed:abstractText
Heterodisulfide reductase (HDR) from methanogenic archaea is an iron-sulfur protein that catalyzes reversible reduction of the heterodisulfide (CoM-S-S-CoB) of the methanogenic thiol-coenzymes, coenzyme M (CoM-SH) and coenzyme B (CoB-SH). Via the characterization of a paramagnetic reaction intermediate generated upon oxidation of the enzyme in the presence of coenzyme M, the enzyme was shown to contain a [4Fe-4S] cluster in its active site that catalyzes reduction of the disulfide substrate in two one-electron reduction steps. The formal thiyl radical generated by the initial one-electron reduction of the disulfide is stabilized via reduction and coordination of the resultant thiol to the [4Fe-4S] cluster.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
386
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
961-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster.
pubmed:affiliation
Max-Planck-Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse, D-35043 Marburg, Germany. hedderic@staff.uni-marburg.de
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't