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Co2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
cyanide
-
enzyme contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
CN-
-
enzyme contains four cyanides in its active site, one is bound to the Ni2+, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, the CN- bound to the nickel ion can be irreversibly removed inducing enzyme inhibition by oxygen
CN-
-
enzyme contains four cyanides in its active site, the Ni2+ bound one is responsible for the insensitivity towards oxygen, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, the CN- bound to the nickel ion can be irreversibly removed inducing enzyme inhibition by oxygen
CO
-
bound to the active site, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
CO
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Fe
-
Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO)
Fe
-
Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover
Fe
-
the (CO)3Fe(II) site is octahedral. An octahedral iron and a distorted square pyramidal nickel are linked by three bridging ligands
Fe2+
-
enzyme contains a [Ni-Fe] cluster
Fe2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Fe2+
-
contains iron in the catalytic core
Fe2+
Solidesulfovibrio fructosivorans
-
-
Iron
-
enzyme contains multiple iron-sulfur clusters, [4Fe-4S] or [2Fe-2S]
Iron
-
non-heme iron protein
Iron
-
no increase of activity by addition of Co2+, Mn2+, Ni2+ or Fe2+
Iron
-
11.5 iron atoms per enzyme molecule, enzyme contains 2 [4Fe-4S] and 2 [2Fe-2S] clusters
Iron
-
the diaphorase contains 3 [2Fe-2S] cluster, the hydrogenase subunit HoxY contains one [2Fe-2S] cluster coordinated by 9 Cys residues
Iron
the active site iron atom has a standard ligation, i.e., one CO and two cyanide ligands
Iron
Hydrogenomonas sp.
-
Fe2+ stabilizes
Iron
-
non-heme iron protein
Iron
-
13.6 iron atoms per enzyme molecule
Iron
-
the enzyme contains at least one [4Fe4S]+ and at least one [2Fe2S]+ cluster
Iron
-
[NiFe] hydrogenases carry a metal centre composed of Fe and Ni atoms at the active site
Iron
-
[NiFe]-hydrogenase, the ratio of iron to nickel is 13 gatom Fe/1 gatom Ni. The absorption spectrum is typical of iron-sulfur proteins having [4Fe-4S] clusters
Mg2+
-
bound to the hydrogenase subunits
Mg2+
Hydrogenomonas sp.
-
stabilizes
Mg2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
Mg2+
-
NAD-reduction: no linear kinetics in absence of metals, 0.5 mM Ni2+ and 5 mM Mg2+ required
Mn2+
Hydrogenomonas sp.
-
stabilizes
Mn2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+, or of high salt concentrations of 500-1500 mM
Ni
-
Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO). The unusual ligation of the Ni by only two thiols plus further (C,O) ligands seems to be a prerequisite of the exceptionally rapid activation of the SH by NADH, involving the loss of an oxygen ligand from the Ni. Evidence for the binding of hydrogen to the open coordination site at Ni has been obtained. The hydrogen cleavage reaction seems not to involve a Ni-C state (Ni(III)-H-). The CN ligand at the Ni may be involved in establishing both rapid activation and oxygen-insensitive catalytic behavior in the SH. Possibly, one important function of the CN is stabilization of the Ni(II) oxidation state throughout the catalytic cycle of hydrogen cleavage
Ni
-
Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover
Ni2+
-
below 0.06 mol Ni2+ per mol of enzyme
Ni2+
-
presence of a Ni(CN)Fe(CN)3(CO) active site is suggested
Ni2+
-
nickel is essential for the catalytic activity of the enzyme
Ni2+
-
2 nickel atoms per enzyme molecule
Ni2+
-
enzyme contains a [Ni-Fe] cluster
Ni2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Ni2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, H2 activation solely takes place on Ni2+
Ni2+
-
contains nickel in the catalytic core
Ni2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
Ni2+
-
highest specific activity with NiCl2, optimal concentration: 1 mM
Ni2+
-
NAD-reduction: no linear kinetics in absence of metals, 0.5 mM Ni2+ and 5 mM Mg2+ required
Ni2+
-
3.8 nickel atoms per enzyme molecule
Ni2+
Solidesulfovibrio fructosivorans
-
-
Ni2+
-
take-up/release of substrates may occur at the Ni site. Flexible coordination structures at Ni may be responsible for the interconversion between H2 and (2H+) as the unique function of the [NiFe] hydrogenase. The coordination mode of the Ni(II) center can vary from square planar, to distorted square pyramidal, and to octahedral geometries, dependent on the nature of the ligands. An octahedral iron and a distorted square pyramidal nickel are linked by three bridging ligands
Nickel
-
[NiFe] hydrogenases carry a metal centre composed of Fe and Ni atoms at the active site
Nickel
-
[NiFe]-hydrogenase, the ratio of iron to nickel is 13 gatom Fe/1 gatom Ni
additional information
-
no increase of activity by addition of Co2+, Mn2+, Ni2+ or Fe2+
additional information
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metalloenzyme
additional information
-
stimulation of activity by salt is greater the less chaotrophic the anion
additional information
metalloenzyme