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A239K
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6% activity of modified soluble wild-type enzyme
A242K
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42% activity of modified soluble wild-type enzyme
G240K
-
63% activity of modified soluble wild-type enzyme
M244K
-
60% activity of modified soluble wild-type enzyme
M247K
-
130% activity of modified soluble wild-type enzyme
N241K
-
38% activity of modified soluble wild-type enzyme
N246K
-
45% activity of modified soluble wild-type enzyme
S286T
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7% activity of wild-type
S286V
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1% activity of wild-type
T243H
-
8% activity of modified soluble wild-type enzyme
T243K
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12% activity of modified soluble wild-type enzyme
T243R
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17% activity of modified soluble wild-type enzyme
H25F
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3% of wild-type kcat
H25F/Y195F
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strong decrease in NOR activity
Y195F
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15% of wild-type kcat
D185A
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
D185E
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
D185N
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
E122A
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substitution leads to an almost complete loss of NOR activity
E122D
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substitution mutant retains 83.2% of the activity of the wild-type enzyme
E122Q
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substitution mutant retains 1.3% of the activity of the wild-type enzyme
E125A
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substitution leads to an almost complete loss of NOR activity
E125D
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substitution leads to an almost complete loss of NOR activity
E125Q
-
substitution mutant retains 13.4% of the activity of the wild-type enzyme
E78F
site-directed mutagenesis, the mutant does not express
K54A
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
N47F
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
N47L
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
Q394M
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
Q398L
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
E198A
-
substitution mutant retains 1.5% of the activity of the wild-type enzyme
E198A
-
the mutation is involved in terminating the proton pathway in the region close to the active site in NOR
E202A
-
70-85% activity of wild-type
E202A
-
substitution mutant retains 39.3% of the activity of the wild-type enzyme
E267A
-
substitution mutant retains 3.6% of the activity of the wild-type enzyme
E267A
-
the mutation is involved in terminating the proton pathway in the region close to the active site in NOR
E58Q
site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type
E58Q
-
the mutation of the NorC subunit slows down the ensuing steady-state NO-reduction as compared to the wild type enzyme
additional information
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norC GRC131 is insensititve to treatment with the Nor inhibitor myxothiazol
additional information
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norC GRC131 is insensititve to treatment with the Nor inhibitor myxothiazol
-
additional information
construction of a truncated soluble domain of NorC, NorC* (DELTAMet1-Val37), by deletion of the 84 5'-terminal nucleotides of gene norC. The mutant NorC exhibits spectra typical of a low-spin heme c. In addition, NorC* functions as the acceptor of an electron from a cytochrome c isolated from the periplasm of Halomonas halodenitrificans and small reducing reagents. The redox potential of NorC* shifted ca. 40mV in the negative direction from that of wild-type NorC. Recombinant NOR exhibits the same spectroscopic properties and reactivity to NO and O2 as wil-type NOR, although its enzymatic activity toward NO is considerably decreased
additional information
-
construction of a truncated soluble domain of NorC, NorC* (DELTAMet1-Val37), by deletion of the 84 5'-terminal nucleotides of gene norC. The mutant NorC exhibits spectra typical of a low-spin heme c. In addition, NorC* functions as the acceptor of an electron from a cytochrome c isolated from the periplasm of Halomonas halodenitrificans and small reducing reagents. The redox potential of NorC* shifted ca. 40mV in the negative direction from that of wild-type NorC. Recombinant NOR exhibits the same spectroscopic properties and reactivity to NO and O2 as wil-type NOR, although its enzymatic activity toward NO is considerably decreased