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SO32- + H2O + 2 oxidized cytochrome c
SO42- + 2 reduced cytochrome c + 2 H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
sulfite + 2 ferrocene methanol + H2O
sulfate + 2 reduced ferrocene methanol + 2 H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c550 + H+
sulfite + H2O + acceptor
sulfate + reduced acceptor + 2 H+
-
-
-
-
?
additional information
?
-
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
in the absence of the core thiosulfate oxidizing multi-enzyme system, enzyme catalyzes sulfide-dependent reduction of Chlorobaculum tepidum cytochrome c-554
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
enzyme is involved in thiosulfate oxidation
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
3-5% of the activity with ferricytochrome
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
-
SDH exhibits a high affinity for both sulfite and the electron acceptor cytochrome c and the reaction follows a ping-pong mechanism
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
horse heart cytochrome or yeast cytochrome
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
ferricytochrome c is the physiological electron acceptor
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
ferricytochrome c is the physiological electron acceptor
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
enzyme is essential for growth with thiosulfate, essential role in lithotrophic sulfur oxidation
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
the enzyme is involved in oxidation of thiosulfate
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
the enzyme is a component of a thiosulfate-oxidizing system
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
specific for sulfite
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
cytochrome c from horse heart
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
oxidative phosphorylation is coupled to sulfite oxidation with a low P/O ratio
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
horse heart cytochrome or yeast cytochrome
-
-
?
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c550 + H+
-
-
-
-
?
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c550 + H+
-
-
-
-
r
additional information
?
-
-
present in taurine-grown cells and effectively absent in acetate grown cells, can be anticipated in both sulfite-generating pathways
-
-
?
additional information
?
-
-
favorable protein-protein interactions between SorT and c-type cytochrome SorU, i.e. Smc04048, lead to productive electron transfer and catalytic activity. No activity with ferrous horse heart cytochrome c, and no activity with O2 as an sulfite oxidase
-
-
?
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0.0018 - 2.1
ferricytochrome c
0.0025
ferricytochrome c550
-
-
-
0.02
ferricyanide
-
pH 8.0
0.58
ferricyanide
-
reaction with ferricyanide or cytochrome c
0.0018
ferricytochrome c
-
-
0.0023
ferricytochrome c
-
recombinant enzyme
0.004
ferricytochrome c
-
-
0.013
ferricytochrome c
-
-
0.019
ferricytochrome c
-
-
2.1
ferricytochrome c
pH 7.8, 25°C
0.000004
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant Y236F
0.000007
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant Y236F
0.0006
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
0.0011
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
0.002
sulfite
-
pH 6.5, reaction with cytochrome c
0.0026
sulfite
-
tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
0.0037
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
0.00456
sulfite
-
wild type enzyme, pH 7.0, using ferricyanide as the electron acceptor
0.006
sulfite
-
mutant enzyme P105A, in 20 mM Tris acetate, pH 8.0, at 25°C
0.00605
sulfite
-
mutant enzyme G473A, pH 7.0, using ferricyanide as the electron acceptor
0.0071
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
0.01
sulfite
-
reaction with yeast ferricytochrome c
0.0111
sulfite
-
wild type enzyme, in 20 mM Tris acetate, pH 8.0, at 25°C
0.012
sulfite
-
at pH 7.7 and 294 mV
0.0125
sulfite
-
at pH 7.7 and 360 mV
0.0149
sulfite
-
wild type enzyme, pH 8.6, using ferricyanide as the electron acceptor
0.022
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
0.026
sulfite
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
0.026
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant Y236F
0.032
sulfite
-
recombinant enzyme
0.032
sulfite
-
mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
0.033
sulfite
-
mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
0.04
sulfite
-
pH 8.0, reaction with cytochrome c
0.042
sulfite
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
0.042
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F
0.054
sulfite
-
at pH 8.0 and 345 mV
0.06
sulfite
-
reaction with cytochrome c
0.063
sulfite
-
at pH 8.0 and 264 mV
0.086
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme
0.114
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant Y236F
0.189
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant H57A
0.191
sulfite
-
mutant enzyme G473A, pH 8.5, using ferricyanide as the electron acceptor
0.22
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant H57A
0.269
sulfite
-
at pH 8.5 and 345 mV
0.27
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant H57A
0.283
sulfite
-
at pH 8.5 and 283 mV
0.29
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant H57A
0.324
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
0.332
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236Fyme
0.452
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant H57A
0.54
sulfite
-
reaction with ferricyanide
0.58
sulfite
-
reaction with cytochrome c
0.667
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant H57A
0.812
sulfite
25°C, 20 mM Tris acetate buffer, pH 5.8, mutant R55M
1
sulfite
-
reaction with ferricyanide
1.087
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M
1.155
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F
1.46
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant H57A
1.63
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M
1.66
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
1.95
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant R55M
3.39
sulfite
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
3.62
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant R55M
4.456
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant Y236F
8.17
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.9, mutant R55M
12.2
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant H57A
15.49
sulfite
25°C, 20 mM Tris acetate buffer, pH 10.0, mutant Y236F
21.2
sulfite
-
mutant enzyme G473W, pH 7.0, using ferricyanide as the electron acceptor
24
sulfite
-
mutant enzyme G473W, pH 8.5, using ferricyanide as the electron acceptor
26.5
sulfite
-
mutant enzyme G473D, pH 7.0, using ferricyanide as the electron acceptor
41.4
sulfite
-
mutant enzyme G473D, pH 8.5, using ferricyanide as the electron acceptor
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10880
ferricytochrome c
-
recombinant enzyme
0.4
sulfite
-
mutant enzyme Y236F, in 20 mM Tris-acetate buffer pH 8.0
0.8
sulfite
-
mutant enzyme Y236F, in 20 mM bis-Tris-acetate buffer pH 6.0
2 - 3.7
sulfite
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
10.6
sulfite
-
tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
26.9
sulfite
-
wild type enzyme, in 20 mM Tris acetate, pH 8.0, at 25°C
33.51
sulfite
-
wild type enzyme, in 20 mM bis-Tris-acetate buffer pH 6.0
35
sulfite
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
36.19
sulfite
-
mutant enzyme Y236F, in 20 mM bis-Tris-acetate buffer pH 6.0
36.8
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant Y236F
39
sulfite
-
mutant enzyme P105A, in 20 mM Tris acetate, pH 8.0, at 25°C
40
sulfite
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
41.6
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant Y236F
46
sulfite
-
mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
48.3
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F
50
sulfite
-
mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
51.8
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant Y236F
52.51
sulfite
-
mutant enzyme Y236F, in 20 mM Tris-acetate buffer pH 8.0
52.7
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant Y236F
53.4
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant Y236F
58.3
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236F
63.5
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
64
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M
64
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M
64
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F
66.3
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant R55M
68.3
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant R55M
70.5
sulfite
25°C, 20 mM Tris acetate buffer, pH 5.8, mutant R55M
73.4
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.9, mutant R55M
86.2
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
88.8
sulfite
25°C, 20 mM Tris acetate buffer, pH 10.0, mutant Y236F
148.4
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant H57A
158.8
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
192.5
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant H57A
214.5
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant H57A
214.6
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant H57A
220.5
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant H57A
222.4
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant H57A
226.5
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant H57A
238.8
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant H57A
293.4
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
333.7
sulfite
-
wild type enzyme, in 20 mM Tris-acetate buffer pH 8.0
345.3
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
410
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme
431
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
519
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
10880
sulfite
-
recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.84
sulfite
25°C, 20 mM Tris acetate buffer, pH 10.0, mutant Y236F
8.98
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.9, mutant R55M
11.6
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant Y236F
18.9
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant R55M
34
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant R55M
54.5
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F
58.9
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M
67.7
sulfite
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
86.8
sulfite
25°C, 20 mM Tris acetate buffer, pH 5.8, mutant R55M
122
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant H57A
132
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant H57A
173
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236F
251
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
358
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant H57A
461
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant Y236F
492
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant H57A
782
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant H57A
799
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant H57A
950
sulfite
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
1010
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant H57A
1130
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant H57A
1140
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F
1400
sulfite
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
1500
sulfite
-
mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
1500
sulfite
-
mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
1500
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
1970
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant Y236F
2400
sulfite
-
wild type enzyme, in 20 mM Tris acetate, pH 8.0, at 25°C
3930
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M
4100
sulfite
-
tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
4880
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme
5600
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant Y236F
6100
sulfite
-
mutant enzyme P105A, in 20 mM Tris acetate, pH 8.0, at 25°C
8420
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant Y236F
15300
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
40300
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
42700
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
75500
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
106000
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
R212A/G473D
-
mutant is able to oligomerize but has undetectable activity, significant random-coil formation
R78K
the active site mutant is catalytically competent in sulfite oxidation activity
R78M
the active site mutant is catalytically competent in sulfite oxidation activity
R78Q
the active site mutant is catalytically competent in sulfite oxidation activity
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
R55Q
-
heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected
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
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
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
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
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
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
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