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EC Number
Metals/Ions
Commentary
Reference
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
Co2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Fe
enzyme contains 1 atom of Fe
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
Fe2+
bacterially expressed AsARD1 preferentially binds Fe2+ rather than Ni2+
Fe2+
dependent on, acireductone dioxygenase 1 is an active metalloenzyme, Fe2+ is active site bound
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
Fe2+
Fe2+ can be replaced by Mg2+, albeit with lower activity
Fe2+
Fe2+-form of enzyme, less than 1 mol per mol of protein
Fe2+
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Results 1 - 10 of 14 > >>