EC Number   |
Protein Variants |
Reference |
|---|
    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 | 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 | 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 | 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 | 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 | 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 | R212A/G473D |
mutant is able to oligomerize but has undetectable activity, significant random-coil formation |
667714 |
| 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 | 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 |
