Linked Life Data

12039013

Source:http://linkedlifedata.com/resource/pubmed/id/12039013

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-5-31
pubmed:abstractText
Some of the principal physical features of iron-sulfur clusters in proteins are analyzed, including metal-ligand covalency, spin polarization, spin coupling, valence delocalization, valence interchange and small reorganization energies, with emphasis on recent spectroscopic and theoretical work. The current state of structural, spectroscopic, and computational knowledge for the iron-sulfur clusters in the nitrogenase iron and iron-molybdenum proteins is examined by comparison and contrast to 'simpler' ironclusters. The differing interactions of the nitrogenase iron and iron-molybdenum clusters compared with those of other iron-sulfur clusters with the protein and solvent environment are also explored.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1367-5931
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
259-73
pubmed:dateRevised
2009-8-25
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Insights into properties and energetics of iron-sulfur proteins from simple clusters to nitrogenase.
pubmed:affiliation
Department of Molecular Biology, TPC15, The Scripps Research Institute, La Jolla, California 92037, USA. lou@scripps.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review