Linked Life Data

20230002

Source:http://linkedlifedata.com/resource/pubmed/id/20230002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
2010-3-31
pubmed:abstractText
The active site of the [FeFe] hydrogenases contains two Fe ions bound to one Cys ligand, three CO molecules, two CN(-) ions, and a dithiolate ligand. The nature of the last of these has been much discussed, and it has been suggested that it contains C, N, or O as the bridgehead atom. Most experimental studies indicate a N atom, whereas a recent density functional theory (DFT) study of a crystal structure indicated an O atom. Here, we performed quantum refinement on the same crystal structure with five different models of the dithiolate ligand X(CH(2)S(-))(2), with X = CH(2), NH(2)(+), NH (two conformations), or O; we found that structures with a N bridgehead atom actually provide the best fit to the raw crystallographic data. Quantum refinement is standard crystallographic refinement in which the molecular mechanics force field normally used to supplement the experimental raw data to give a more chemical structure is replaced by more accurate DFT calculations for the active site. Thereby, we obtain structures that are an ideal compromise between DFT and crystallography.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
132
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4512-3
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Quantum refinement of [FeFe] hydrogenase indicates a dithiomethylamine ligand.
pubmed:affiliation
Theoretical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden. Ulf.Ryde@teokem.lu.se
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't