EC Number |
Metals/Ions |
Reference |
---|
1.12.1.2 | CN- |
- |
706499 |
1.12.1.2 | 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 |
655890 |
1.12.1.2 | 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 |
654562, 656298 |
1.12.1.2 | CO |
- |
706499 |
1.12.1.2 | CO |
bound to the active site, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre |
654562, 656298 |
1.12.1.2 | CO |
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre |
655890 |
1.12.1.2 | 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 |
439702 |
1.12.1.2 | cyanide |
enzyme contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen |
656298 |
1.12.1.2 | Fe |
Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO) |
674165 |
1.12.1.2 | Fe |
Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover |
672067 |