1.13.99.1	Fe2+	1 mM	671152, 676819	
1.13.99.1	Fe2+	1 mM Fe(II) + 4 mM quinolinate activate to 70% of the Fe(II)/cysteine system, Fe(II) alone causes very little activation, quinolinate gives considerable activation in absence of Fe(II), activation by Fe(II) and quinolinate is very temperature dependent	6866	
1.13.99.1	Fe2+	1 mM Fe(II) and 2 mM cysteine	6866, 6874	
1.13.99.1	Fe2+	1 mM Fe2+ plus 2mM cysteine required	172313	
1.13.99.1	Fe2+	2 mM used in assay conditions	764595	
1.13.99.1	Fe2+	best activation system	6866	
1.13.99.1	Fe2+	contains iron most probably in divalent form, enzyme consisting of 16 subunits contains 8 iron atoms per molecule	6870	
1.13.99.1	Fe2+	either reagent alone gives very little activation	6874	
1.13.99.1	Fe2+	iron protein	6869, 6870	
1.13.99.1	Fe2+	less active preparations: 1.5 atoms of iron per molecule	6869	
1.13.99.1	Fe2+	most active preparation: 4 mol of iron per 65000 MW protein	6869	
1.13.99.1	Fe2+	no other metal ion can replace Fe(II)	6874	
1.13.99.1	Fe2+	nonheme iron enzyme	6875	
1.13.99.1	Iron	contains a non-heme dinuclear iron cluster, observations implicate the mixed-valent, diiron-(II/III) form of the enzyme as the active state	672164	
1.13.99.1	Iron	diiron cluster	687712	
1.13.99.1	Iron	dinuclear iron cluster	672163	
1.13.99.1	Iron	enzyme contains non-heme iron	660234	
1.13.99.1	Iron	the mixed-valent, II/III state of iron, rather than the conventional II/II state, activates O2 for D-glucuronate production in the MIOX reaction	676860	
1.13.99.1	Iron	uses its dinuclear iron cluster to activate O2 for cleavage of myo-inositol that binds to the mixed-valence diiron center via a bridging alkoxide	674174