1.13.11.50	Cu2+	20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate	19	
1.13.11.50	EDTA	largely irreversible losses	21	
1.13.11.50	H2O2	0.1 mM, immediate and total inhibition	22	
1.13.11.50	H2O2	1 M H2O2 causes complete loss of enzyme activity in less than 10 min, contains no Fe2+ (probably oxidized to Fe3+), partial reconstitution (40%) with 2 mM Fe2+, 20 mM Tris/HCl buffer, pH 7.5, 25°C	22	
1.13.11.50	hexacyanoferrate(III)	2.5 mM, 80% decrease in activity within 10 min	51693	
1.13.11.50	KCN	largely irreversible losses	161	
1.13.11.50	Mn2+	20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate	11	
1.13.11.50	additional information	no inactivation effect of Fe3+	2	
1.13.11.50	Ni2+	20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate	38	
1.13.11.50	o-phenanthroline	largely irreversible losses	239	
1.13.11.50	Zn2+	20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate	14