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Zoekopdracht: faculteit: "FNWI" en publicatiejaar: "2004"

AuteursH.P. van der Linden, T. Burgdorf, M. Bernhard, B. Bleijlevens, B. Friedrich, S.P.J. Albracht
TitelThe soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its activer site, one of which is responsible for the insensitivity towards oxygen.
TijdschriftJBIC. Journal of biological inorganic chemistry
Jaargang9
Jaar2004
Pagina's616-626
ISSN09498257
FaculteitFaculteit der Natuurwetenschappen, Wiskunde en Informatica
Instituut/afd.FNWI: Swammerdam Institute for Life Sciences (SILS)
TrefwoordenCyanide ligand; 15N enrichment; [NiFe]-hydrogenase; Oxygen sensitivity; Knallgas bacterium
Basisclassificatie35.75 Biochemistry: proteins, nuclein acids
SamenvattingInfrared spectra of 15N-enriched preparations of the soluble cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha are presented. These spectra, together with chemical analyses, show that the Ni-Fe active site contains four cyanide groups and one carbon monoxide molecule. It is proposed that the active site is a (RS)2(CN)Ni(-RS)2Fe(CN)3(CO) centre (R=Cys) and that H2 activation solely takes place on nickel. One of the two FMN groups (FMN-a) in the enzyme can be reversibly released upon reduction of the enzyme. It is now reported that at longer times also one of the cyanide groups, the one proposed to be bound to the nickel atom, could be removed from the enzyme. This process was irreversible and induced the inhibition of the enzyme activity by oxygen; the enzyme remained insensitive to carbon monoxide. The Ni-Fe active site was EPR undetectable under all conditions tested. It is concluded that the Ni-bound cyanide group is responsible for the oxygen insensitivity of the enzyme.
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