1.7.2.2: nitrite reductase (cytochrome; ammonia-forming)
This is an abbreviated version!
For detailed information about nitrite reductase (cytochrome; ammonia-forming), go to the full flat file.
Word Map on EC 1.7.2.2
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1.7.2.2
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six-electron
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desulfovibrio
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dissimilatory
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succinogenes
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wolinella
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nitrosomonas
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ammonification
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thioalkalivibrio
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nitratireducens
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desulfuricans
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chromatium
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flavorubredoxin
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deleyianum
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menaquinol
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hydrogenobacter
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pentahaem
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hildenborough
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sulfurospirillum
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ferrocytochrome
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flavohemoglobins
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cxxch
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analysis
- 1.7.2.2
-
six-electron
- desulfovibrio
-
dissimilatory
- succinogenes
-
wolinella
- nitrosomonas
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ammonification
- thioalkalivibrio
- nitratireducens
- desulfuricans
- chromatium
- flavorubredoxin
- deleyianum
- menaquinol
- hydrogenobacter
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pentahaem
- hildenborough
- sulfurospirillum
- ferrocytochrome
- flavohemoglobins
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cxxch
- analysis
Reaction
Synonyms
ammonia-forming cytochrome c nitrite reductase, ccNiR, CcuHao, CfHao, CmHao, cNiR, cytochrome c NiR, cytochrome c nitrite reductase, cytochrome c nitrite reductase complex, cytochrome c-552, epsilonHao, epsilonproteobacterial hydroxylamine oxidoreductase, Glov_1042, haoA, hexaheme c-type cytochrome, More, multihaem c NiR, multiheme cytochrome c nitrite reductase, multiheme nitrite reductase, NiR, NiR cytochrome c552, nirB, NirC, nitrite reductase, NpHao, NrfA, NrfA2NrfH complex, NrfHA, octahaem cytochrome c nitrite reductase, SCO2486, SCO2488, TvNiR, WS0969
ECTree
1.7.2.2 nitrite reductase (cytochrome; ammonia-forming)Advanced search results
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results (Engineering
Engineering on EC 1.7.2.2 - nitrite reductase (cytochrome; ammonia-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
W434Y
H264N
mutant is unable to catalyze nitrite reduction but able to reduce hydroxylamine. The mutant simultaneously binds nitrite and electrons at the catalytic heme
Q263E
site-directed mutagenesis, the mutation leads to introduction of a negative charge into the vicinity of the active site heme, and the mutant shows reduced activity compared to the wild-type enzyme. The high spin state of the active site to be preserved, indicating that a water/hydroxide molecule is still coordinated to the heme in the resting state of the enzyme
K100H
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mutagenesis of the hem-binding motif CWSCK results in almost complete loss of formate-dependent nitrite reduction
K100I
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mutagenesis of the hem-binding motif CWSCK results in almost complete loss of formate-dependent nitrite reduction
K100L
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mutagenesis of the hem-binding motif CWSCK results in almost complete loss of formate-dependent nitrite reduction
H268M
one of the EPR-silent heme's histidine axial ligands is replaced with a methionine
K119H
site-directed mutagensis, mutation of the essential lysine residue of the non-canonical HBM (CX2CK), inactive mutant. The mutant NrfA protein displays a similar pattern of rapid degradation like the wild-type without maturation
K119L
site-directed mutagensis, mutation of the essential lysine residue of the non-canonical HBM (CX2CK), inactive mutant. The mutant NrfA protein displays a similar pattern of rapid degradation like the wild-type without maturation
R277A
Trichlorobacter lovleyi
variant contains all five hemes, less than 3% of wild-type activity
R277K
Trichlorobacter lovleyi
variant contains all five hemes, less than 3% of wild-type activity
R277Q
Trichlorobacter lovleyi
variant contains all five hemes, less than 3% of wild-type activity
R277A
Trichlorobacter lovleyi DSM 17278
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variant contains all five hemes, less than 3% of wild-type activity
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R277K
Trichlorobacter lovleyi DSM 17278
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variant contains all five hemes, less than 3% of wild-type activity
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R277Q
Trichlorobacter lovleyi DSM 17278
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variant contains all five hemes, less than 3% of wild-type activity
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H277N
mutant is unable to catalyze nitrite reduction but able to reduce hydroxylamine. The mutant simultaneously binds nitrite and electrons at the catalytic heme
Y218F
active site mutant, that shows almost complete loss of nitrite reductase activity, while sulfite reduction remains unaffected
H277N
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mutant is unable to catalyze nitrite reduction but able to reduce hydroxylamine. The mutant simultaneously binds nitrite and electrons at the catalytic heme
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additional information
W434Y
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site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation activity, but decreased hydroxylamine reduction and increased nitrite reduction compared to the wild-type enzyme
W434Y
site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation, but slightly reduced hydroxylamine reduction and significantly reduced nitrite reduction compared to the wild-type enzyme
W434Y
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site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation activity, but highly increased hydroxylamine reduction and highly reduced nitrite reduction compared to the wild-type enzyme
additional information
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introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm
additional information
introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm
additional information
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introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm
additional information
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introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm
additional information
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anaerobically grown Escherichia coli nrf mutants are more sensitive to NO radicals than the parent strain
additional information
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effects of all eight possible combinations of norV, hmpA and nrfA single, double and triple mutations, overview. The norV nrfA mutant cannot grow after NO addition
additional information
costruction of a DELTAnrfA mutant enzyme knockout strain, expression of the wild-type enzyme from vector pHG101 can restore the enzyme activity, but not expression of enzyme mutants K119L and K119H
