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Results 1 - 10 of 18 > >>
EC Number
Amino acid exchange
Commentary
Reference
C185A
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
C185S
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
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
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
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
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
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
P105A
the mutant enzyme shows increased catalytic efficiency compared to the wild type enzyme
P105A/P111A
the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme
P111A
the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme
Results 1 - 10 of 18 > >>