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