1.8.2.1	C185A	the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor	711242	
1.8.2.1	C185S	the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor	711242	
1.8.2.1	G473A	mutant is able to dimerize and has steady-state activity comparable to that of the wild type, stopped-flow analysis of the reductive half-reaction of this variant yields a rate constant nearly 3 times higher than that of the wild type	667714	
1.8.2.1	G473D	monomer, mutant is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type, significant random-coil formation	667714	
1.8.2.1	G473W	monomer, mutant with 5fold higher activity than G473D and nearly wild-type activity at pH 7.0 when ferricyanide is the electron acceptor, significant random-coil formation	667714	
1.8.2.1	H57A	heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent	724418	
1.8.2.1	H57A	mutant with reduced activity, Tyr-236 and His-57 are necessary to stabilize Arg-55 in a position for optimal hydrogen bonding to the heme 6-propionate	722663	
1.8.2.1	P105A	the mutant enzyme shows increased catalytic efficiency compared to the wild type enzyme	711223	
1.8.2.1	P105A/P111A	the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme	711223	
1.8.2.1	P111A	the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme	711223	
1.8.2.1	R212A/G473D	mutant is able to oligomerize but has undetectable activity, significant random-coil formation	667714	
1.8.2.1	R55K	heme potential is similar to wild-type, the molybdenum redox potential is not affected. Wild-type and mutant show pH dependence of the electrochemical catalytic halfwave potential	724418	
1.8.2.1	R55M	heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent	724418	
1.8.2.1	R55M	mutant with reduced activity, R-55 is an important position close to the substrate binding site, where it makes hydrogen bonds to the equatorial oxo ligand of the molybdenum, to Gln-33, and a nearby water molecule. It also forms a salt bridge, comprising two hydrogen bonds, with propionate-6 of the heme moiety of the cytochrome subunit	722663	
1.8.2.1	R55Q	heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected	724418	
1.8.2.1	R78K	the active site mutant is catalytically competent in sulfite oxidation activity	764491	
1.8.2.1	R78M	the active site mutant is catalytically competent in sulfite oxidation activity	764491	
1.8.2.1	R78Q	the active site mutant is catalytically competent in sulfite oxidation activity	764491	
1.8.2.1	Y236F	mutant with reduced activity, Tyr-236 and His-57 are necessary to stabilize Arg-55 in a position for optimal hydrogen bonding to the heme 6-propionate	722663	
1.8.2.1	Y236F	near Mo center	700633	
1.8.2.1	Y236F	reduced turnover rates and substrate affinity as well as an altered reactivity toward molecular oxygen as an electron acceptor, unlike the wild type enzyme the mutant enzyme is reoxidized quickly in the presence of molecular oxygen	667744