Linked Life Data

1644180

Source:http://linkedlifedata.com/resource/pubmed/id/1644180

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-9-8
pubmed:abstractText
Methane monooxygenase (MMO) catalyses the biological transformation of methane to methanol at a binuclear iron site. Guided by the three-dimensional structure of the R2 protein of E. coli ribonucleotide reductase (RNR), we have aligned the sequences of two different MMOs with the sequences of the iron coordinating four helix bundle in R2. The model suggests that the central four helix bundle of R2 is present also in MMO. The iron coordination is similar in MMO and R2 with two histidine ligands and four carboxyl ligands in both cases. The residues lining the proposed oxygen binding site in MMO are significantly smaller in MMO than in R2 allowing binding of both molecular oxygen and methane at this site. This binding site is lined by residues Cys151, Thr213, Ile217 and Ile(Val)239.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
307
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
257-62
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase.
pubmed:affiliation
Department of Molecular Biology, Swedish University of Agriculture Sciences, Uppsala.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't