1.13.11.54	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	
1.13.11.54	Co2+	the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53	741923	
1.13.11.54	Fe	enzyme contains 1 atom of Fe	661058	
1.13.11.54	Fe2+	apoenzyme is catalytically inactive. Addition of Fe2+ yields activity. Production of the enzyme in intact Escherichia coli depends on the availability of the Fe2+. Enzyme contains 0.9 Fe2+ per enzyme molecule	662101	
1.13.11.54	Fe2+	bacterially expressed AsARD1 preferentially binds Fe2+ rather than Ni2+	663098	
1.13.11.54	Fe2+	dependent on	764494, 764909	
1.13.11.54	Fe2+	dependent on, acireductone dioxygenase 1 is an active metalloenzyme, Fe2+ is active site bound	725438	
1.13.11.54	Fe2+	dependent on. Fe2+ transmits electrons from the residues, coordinating it to bound dioxygen and populating its formerly p*-orbital. This leads to dioxygen splitting in the second intermediate and eventual access to the Fe2+-dependent acireductone dioxygenase reaction route	725214	
1.13.11.54	Fe2+	Fe2+ can be replaced by Mg2+, albeit with lower activity	675408	
1.13.11.54	Fe2+	Fe2+-form of enzyme, less than 1 mol per mol of protein	743725	
1.13.11.54	Fe2+	Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable	741923	
1.13.11.54	Fe2+	required	764775	
1.13.11.54	Iron	ligands are H96, H98, E102 and H140, the same as in the isoform requiring Ni2+, 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	
1.13.11.54	Mn2+	the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53	741923	
1.13.11.54	additional information	the identity of bound metal ion does not affect the oligomeric state of ARD	741923	
1.13.11.54	Ni2+	the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53	741923