1.13.11.50	Cu2+	sulfate, similar binding as Fe2+ in wild-type enzyme	696107	
1.13.11.50	Fe2+	0.9-1.0 iron atoms per subunit, bound to active enzyme, essential for catalytic activity	636327	
1.13.11.50	Fe2+	active site nonheme monoiron(II) center, facially ligated by three histidine residues, overview. Spectral analysis of Dke1 FeII-alpha-keto acid complexes with 4-hydroxyphneylpyruvate, overview	725198	
1.13.11.50	Fe2+	Dke1 contains an atypical, three-histidine-ligated, mononuclear non-heme Fe2+ center, spectroscopic analysis, overview. Stabilizing effect of Glu98 on the 6C geometry of the metal center, priming it for substrate ligation. Also Thr107 stabilizes the Fe(II) cofactor	711267	
1.13.11.50	Fe2+	essential for activity	671683	
1.13.11.50	Fe2+	Fe2+-dependent enzyme, 1 molecule per subunit	675466	
1.13.11.50	Fe2+	its active site consists of a redox-active iron(II) center	764545	
1.13.11.50	Fe2+	nonheme Fe(II) cofactor, distinct organization of the hydrophilic triad in the free and substrate-ligated wild-type enzyme. In the free species, the Fe(II) center is coordinated to three histidines and one glutamate, whereas the substrate-ligated, catalytically competent enzyme-substrate complex has an Fe(II) center with three-histidine coordination, with a small fraction of three-histidine, one-glutamate coordination	725553	
1.13.11.50	Fe2+	sulfate, necessary for enzyme activity. About 0.9 mol Fe2+/mol wild-type enzyme, less than 5% Fe2+ in mutants except 0.27 mol/mol H104E-enzyme and 0.45 mol/mol H104N-enzyme	696107	
1.13.11.50	Fe2+	the Fe(II) coordinating triad is composed of three His residues, geometric and electronic structure of the Fe(II) center, structure and function comparison with other dioxygenases containing a two histidines and a carboxylate coordinating the iron center in a facial triad, overview	711258	
1.13.11.50	Fe2+	utilizes a non-heme Fe2+ cofactor	674150	
1.13.11.50	Fe2+	variable amounts	636328	
1.13.11.50	Fe3+	citrate, no interference with Fe2+	696107	
1.13.11.50	Iron	an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein. The Fe2+ ion when expelled from the binding site can be trapped at different locations within the enzyme. The neighborhood of residue Glu11 (form the neighbor subunit) is the second most favorable binding site for the Fe2+ ion after the active site	742322	
1.13.11.50	Iron	dependent on, metalloenzyme, 1 iron bound per subunit, required for positioning of the substrate and for rendering of the appropriate electronic environment	657866	
1.13.11.50	Mn2+	sulfate, similar binding as Fe2+ in wild-type enzyme	696107	
1.13.11.50	additional information	spectrophotometrical monitoring, Fe2+ and Fe3+ coordination, formation of iron(II) enzyme-substrate complexes, and detachment kinetics, overview	725553	
1.13.11.50	additional information	the enzyme is a mononuclear non-heme iron enzyme, overview	711258	
1.13.11.50	Ni2+	dependent on	764544	
1.13.11.50	Ni2+	sulfate, similar binding as Fe2+ in wild-type enzyme	696107	
1.13.11.50	Zn2+	sulfate, similar binding as Fe2+ in wild-type enzyme	696107	
1.13.11.50	Zn2+	variable amounts	636328