Linked Life Data

2840063

Source:http://linkedlifedata.com/resource/pubmed/id/2840063

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-8-18
pubmed:abstractText
The purification of the hydroxylase component of a 3 component methane monooxygenase from the type II methanotroph Methylosinus trichosporium OB3b is reported. The enzyme (240 kDa) has an (alpha beta gamma)2 subunit structure as observed for hydroxylases isolated from other Type I and Type II methanotrophs, but it exhibits a 5 to 10 fold higher specific activity and is isolated in 2 to 10 fold higher yield. EPR and Mössbauer spectra of the hydroxylase show that it contains a coupled iron center containing an even number of iron atoms. The spectra are similar to those of proteins known to contain oxo-bridged binuclear iron centers. The presence of such a center is unprecedented in a monooxygenase and suggests that a novel mechanism is utilized.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-70
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Purification of a high specific activity methane monooxygenase hydroxylase component from a type II methanotroph.
pubmed:affiliation
Department of Biochemistry, Medical School, University of Minnesota, Minneapolis 55455.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.