Linked Life Data

2545689

Source:http://linkedlifedata.com/resource/pubmed/id/2545689

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1989-8-14
pubmed:abstractText
Crystals of trimethylamine dehydrogenase have been examined by difference Fourier methods at 6.0-A resolution after partial reduction by substrate and by dithionite in the presence of inhibitor. Similar studies of the inhibited oxidized enzyme and of the enzyme reduced fully by dithionite alone were also carried out. In all cases ligand binding at the active site occurred. In addition, there were small structural changes, possibly side chain movements, in the inhibited oxidized enzyme and somewhat larger changes in the partially reduced crystals. The largest changes occurred with the fully reduced enzyme. However, in no cases were subunit or domain movements observed nor were changes observed in the position of the FMN or [4Fe-4S] cofactors. Parallel studies of crystalline trimethylamine dehydrogenase were carried out by EPR spectroscopy. The results show that the electronic states of the crystalline enzyme under the conditions of the difference Fourier studies are comparable to those which occur in solution under similar conditions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11887-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Studies of crystalline trimethylamine dehydrogenase in three oxidation states and in the presence of substrate and inhibitor.
pubmed:affiliation
Department of Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.