Linked Life Data

8198565

Source:http://linkedlifedata.com/resource/pubmed/id/8198565

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-6-29
pubmed:abstractText
In spite of their structural and amino acid sequence differences, Fe-only and Ni-containing hydrogenases achieved the same catalytic reactions. A chemical modification of histidine residues using a highly specific reagent (pentaammineruthenium II) has been carried out on Desulfovibrio vulgaris Hildenborough Fe-hydrogenase and Desulfovibrio desulfuricans Norway Ni-Fe-Se-hydrogenase. The preliminary results obtained suggest the existence of a general mechanism involving histidine residues in the two groups of hydrogenases. These residues may be part of the histidine-containing motive shown to be present in both Fe- and Ni-Fe-hydrogenase sequences by Hydrophobic Cluster Analysis. This analysis also allows us to suggest a functional role for the small subunit of Desulfovibrio vulgaris Hildenborough Fe-hydrogenase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
201
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
128-34
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Involvement of histidine residues in the catalytic mechanism of hydrogenases.
pubmed:affiliation
Laboratoire de Chimie Bactérienne, Centre National de la Recherche Scientifique (CNRS), Marseille, France.
pubmed:publicationType
Journal Article, Comparative Study