4.4.1.3	Ca2+	-	747144	
4.4.1.3	Cobalt	DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM	749057	
4.4.1.3	copper	DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM	749057	
4.4.1.3	Iron	isolated protein contains 0.5 Fe per subunit. The UV-visible spectrum exhibits a feature at 550 nm, consistent with a tyrosinate-Fe(III) ligand-to-metal charge transfer transition. Both the Fe(III) oxidized and Fe(II) reduced species are active	747110	
4.4.1.3	Iron	the as-isolated enzyme contains 0.2-0.4 equivalents of bound iron. DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM, with Mn(II) and Fe(III) exhibiting weaker binding affinities. The presence of Fe(II) or Mn(II) elicits an about 40fold increase in DddW lyase activity compared to the apo-enzyme	749057	
4.4.1.3	Manganese	the presence of Fe(II) or Mn(II) elicits an about 40fold increase in DddW lyase activity compared to the apo-enzyme	749057	
4.4.1.3	Mn2+	-	747144	
4.4.1.3	additional information	none of the metals Co, Cu, Mn, Ni or Zn is detected at above background levels	716137	
4.4.1.3	Nickel	DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM	749057	
4.4.1.3	Zinc	Zn2+ is bound at the active site	748399