Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-12-2
pubmed:abstractText
Site-directed mutagenesis of amino acid residues proximate to the active site of the Ni-Fe hydrogenase of Desulfovibrio fructosovorans has been done. The different mutants have been analyzed by FTIR spectroscopy and compared with wild type enzyme. The changes observed in the spectra confirm that hydrogen bonds between the CN(-) ligands of the active site's Fe atom and certain neighbor amino acid residues stabilize the active center within the protein matrix. However, kinetic analysis of the mutants indicates that none of the replaced residues have an important role in the catalytic mechanism of the hydrogenase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0949-8257
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-34
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovoransNi-Fe hydrogenase.
pubmed:affiliation
Instituto de Catalisis, CSIC, Campus de Cantoblanco, 28049 Madrid, Spain. alopez@icp.csic.es
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't