1.13.11.53	Co2+	apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule	662101	
1.13.11.53	Co2+	Co2+-form of enzyme, about 1 mol per mol of protein	743725	
1.13.11.53	Co2+	Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable	741923	
1.13.11.53	Co2+	quantum-classical dynamics simulations with Co2+ bound. both Fe2+-like (reaction of EC 1.13.11.54) and Ni2+-like (reaction of EC 1.13.11.53) routes are accessible to Co2+-ARD, but the mechanism involves a bifurcating transition state, and so the exact product distribution is determined by the reaction dynamics	742270	
1.13.11.53	Fe2+	the Fe2+ bound protein catalyzes the reaction of EC 1.13.11.54	741923	
1.13.11.53	Iron	the enzyme contains a non-heme, iron-binding site critical for its activity	764226	
1.13.11.53	Mg2+	required	662091	
1.13.11.53	Mn2+	Mn2+-form of enzyme, less than 1 mol per mol of protein	743725	
1.13.11.53	Mn2+	Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable	741923	
1.13.11.53	additional information	the identity of bound metal ion does not affect the oligomeric state of ARD	741923	
1.13.11.53	Ni2+	-	663098, 673849, 677051	
1.13.11.53	Ni2+	apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule	662101	
1.13.11.53	Ni2+	dependent on	725214, 765728	
1.13.11.53	Ni2+	enzyme contains 1 atom of Ni	661058	
1.13.11.53	Ni2+	enzyme contains Ni2+	662471	
1.13.11.53	Ni2+	model for the solution structure of the paramagnetic Ni2+-containing enzyme	662473	
1.13.11.53	Ni2+	Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable	741923	
1.13.11.53	Ni2+	Ni2+ can be conservatively replaced by Mn2 +or Co2+, giving rise to ARD activity (CO production)	675408	
1.13.11.53	Ni2+	Ni2+-containg enzyme	661942	
1.13.11.53	Ni2+	Ni2+-form of enzyme, less than 1 mol per mol of protein	743725	
1.13.11.53	Ni2+	required	764433	
1.13.11.53	Ni2+	required for activity	674007	
1.13.11.53	Ni2+	solution structure of the nickel-containing enzyme is determined using NMR methods. X-ray absorption spectroscopy, assignment of hyperfine shifted NMR resonance and conserved domain homology are used to model the metal-binding site because of the paramagnetism of the bound Ni2+	662933	
1.13.11.53	Ni2+	structure of the Ni site in resting Ni-ARD as containing a six coordinate Ni site composed of O/N-donor ligands including 3-4 histidine residues. The substrate binds to the Ni center in a bidentate fashion by displacing two ligands, at least one of which is a histidine ligand	661059	
1.13.11.53	Nickel	detection of one-bond 15N-13Calpha correlations in the vicinity of the paramagnetic Ni2+	687303	
1.13.11.53	Nickel	ligands are H96, H98, E102 and H140, the same as in the isoform requiring Fe2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions	685212	
1.13.11.53	Zn2+	Zn2+-form of enzyme, less than 1 mol per mol of protein	743725