Information on EC 1.7.2.4 - nitrous-oxide reductase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY
1.7.2.4
-
RECOMMENDED NAME
GeneOntology No.
nitrous-oxide reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nitrogen + H2O + 2 ferricytochrome c = nitrous oxide + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
nitrate reduction I (denitrification)
-
nitrate reduction VII (denitrification)
-
nitrifier denitrification
-
Nitrogen metabolism
-
SYSTEMATIC NAME
IUBMB Comments
nitrogen:cytochrome c oxidoreductase (N2O-forming)
The reaction is observed only in the direction of nitrous oxide reduction. Contains the mixed-valent dinuclear CuA species at the electron entry site of the enzyme, and the tetranuclear Cu-Z centre in the active site. In Paracoccus pantotrophus, the electron donor is cytochrome c552.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
HdN2OR
Hyphomicrobium denitrificans A3151
-
-
-
multicopper oxidase
-
-
N(2)OR
-
-
-
-
N2O reductase
-
-
-
-
N2O reductase
P94127
-
N2O reductase
-
-
N2O reductase
Bradyrhizobium japonicum USDA110
-
-
-
N2O reductase
-
-
N2O reductase
Ensifer adhaerens SN611
-
-
-
N2O reductase
-
-
N2O reductase
-
-
N2O reductase
Pseudomonas denitrificans CCUG 2519
-
-
-
N2O reductase
Q9F0W4
-
N2O reductase
Pseudomonas fluorescens C7R12
Q9F0W4
-
-
N2O reductase
-
-
N2O reductase
Sinorhizobium meliloti 50
-
-
-
N2OR
Achromobacter cycloclastes IAM1013
P94127
-
-
nitrous oxide reductase
-
-
-
-
nitrous oxide reductase
-
-
nitrous oxide reductase
P94127
-
nitrous oxide reductase
Achromobacter cycloclastes IAM1013
P94127
-
-
nitrous oxide reductase
-
-
nitrous oxide reductase
Bradyrhizobium japonicum USDA110
-
-
-
nitrous oxide reductase
Q19Q69
-
nitrous oxide reductase
Q51705
-
nitrous oxide reductase
-
-
nitrous oxide reductase
-
-
nitrous oxide reductase
-
-
NosZ
Q89XJ6
catalytic subunit of nitrous oxide reductase
NosZ
Bradyrhizobium japonicum USDA110
-
-
-
NosZ
Ensifer adhaerens SN611
-
-
-
NosZ
Q51705
gene name
NosZ
Pseudomonas denitrificans CCUG 2519
-
-
-
NosZ
Pseudomonas fluorescens C7R12
Q9F0W4
-
-
NosZ
-
-
-
NosZ
Pseudomonas stutzeri ATCC 14405
P19573
-
-
NosZ
Sinorhizobium meliloti 50
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
55576-44-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 21921
-
-
Manually annotated by BRENDA team
strain IAM1013
UniProt
Manually annotated by BRENDA team
Achromobacter cycloclastes 1013
strain 1013
UniProt
Manually annotated by BRENDA team
Achromobacter cycloclastes IAM1013
strain IAM1013
UniProt
Manually annotated by BRENDA team
NCIMB 11015, X-ray scattering data, 20 A resolution
-
-
Manually annotated by BRENDA team
strain ATCC 8750
-
-
Manually annotated by BRENDA team
strain 562 and strain USDA110
-
-
Manually annotated by BRENDA team
strain USDA110
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum USDA110
strain USDA110
-
-
Manually annotated by BRENDA team
strain DSM 15892T
-
-
Manually annotated by BRENDA team
strain SN611
-
-
Manually annotated by BRENDA team
Ensifer adhaerens SN611
strain SN611
-
-
Manually annotated by BRENDA team
strain DSM 15936T
-
-
Manually annotated by BRENDA team
strain DSM 1869
-
-
Manually annotated by BRENDA team
Hyphomicrobium denitrificans A3151
A3151
-
-
Manually annotated by BRENDA team
Marinobacter hydrocarbonoclasticus 617
strain 617
-
-
Manually annotated by BRENDA team
formerly Thiosphaera pantotropha
-
-
Manually annotated by BRENDA team
formerly Thiosphaera pantotropha; LMD 82.5
-
-
Manually annotated by BRENDA team
Paracoccus pantotrophus LMD 82.5
LMD 82.5
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa P2
strain P2
-
-
Manually annotated by BRENDA team
strain CCUG 2519
-
-
Manually annotated by BRENDA team
Pseudomonas denitrificans CCUG 2519
strain CCUG 2519
-
-
Manually annotated by BRENDA team
precursor; strain C7R12
SwissProt
Manually annotated by BRENDA team
Pseudomonas fluorescens C7R12
precursor; strain C7R12
SwissProt
Manually annotated by BRENDA team
strain ED3
-
-
Manually annotated by BRENDA team
strain G59
-
-
Manually annotated by BRENDA team
strain ED3
-
-
Manually annotated by BRENDA team
Pseudomonas sp. G59
strain G59
-
-
Manually annotated by BRENDA team
wild-type, C622D-mutant laccking copper in the CuA-site and N2OR V a mutant which lacks CuZ
-
-
Manually annotated by BRENDA team
Pseudomonas stutzeri ATCC 14405
-
UniProt
Manually annotated by BRENDA team
strain 8A55
-
-
Manually annotated by BRENDA team
Rhizobium sp. 8A55
strain 8A55
-
-
Manually annotated by BRENDA team
strains N22, Kb1
-
-
Manually annotated by BRENDA team
f. sp. denitrificans IL106
-
-
Manually annotated by BRENDA team
strain 2.4.1
-
-
Manually annotated by BRENDA team
Rhodopseudomonas palustris PW5
strain PW5
-
-
Manually annotated by BRENDA team
Rhodospirillum rubrum S1
stain S1
-
-
Manually annotated by BRENDA team
strain 1021; strain 50
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti 50
strain 50
-
-
Manually annotated by BRENDA team
ATCC 29591
-
-
Manually annotated by BRENDA team
under anaerobic conditions cytochrome c oxidase activity is observed
-
-
Manually annotated by BRENDA team
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cupredoxin
-
a copper enzyme with cupredoxin containing blue T1 copper and red T2 copper. Blue and red copper centers form initially before they are pH-dependently transformed into purple CuA center, lower pH resulting in fewer trapped T1 and T2 coppers and faster transition. Structure overview
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TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8
-
N2O
-
pH 7.6, 25°C
162.9
-
reduced benzyl viologen
-
pH 7.1, temperature not specified in the publication
89.3
-
reduced pseudoazurin
-
pH 7.1, temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
242
-
Fe2+
-
pH 7.6, 25°C
0
250
-
N2O
-
pH 7.6, 25°C
14203
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.028
-
Acetylene
-
non competitive
0.035
-
Acetylene
-
-
0.0035
-
CO
-
non competitive
0.000045
-
KCN
-
non competitive
0.00035
-
NaN3
-
non competitive
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
10.6
P94127
perturbations of the protein conformation induced by pH variations, although the principal secondary structure elements are largely unaltered
5.7
9.4
-
pH profile with two maxima, high complexity of pH dependence, overview
6
9.2
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half maximum activity values at pH 6 and pH 9.2
7
9.5
-
approx. 50% of maximal activity at pH 7.5, approx. 75% of maximal activity at pH 9.5
9
10
-
activity is maximal after incubation at high pH values
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
85
-
activity is maximal after exposure to high temperatures
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
the purple form of enzyme, in which the copper centre is in the oxidized [2Cu2+:2Cu+] redox state, is redox active, although it is still catalytically non-competent, as its specific activity is lower than that of the activated fully reduced enzyme and comparable with that of the enzyme with the copper centre in either the [1Cu2+:3Cu+] redox state or in the redox inactive state
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapour diffusion method
P94127
2.4 A resolution, preliminary study
-
1.6 A resolution
-
building of two models of the active site reveals two distinct mechanisms. In the first model, N2O binds to the fully reduced tetranuclear Cu4S core in a bent my-(1,3)-O,N bridging fashion between the CuI and CuIV centres and subsequently extrudes N2 while generating the corresponding bridged my-oxo species. In the second model, substrate N2O binds loosely to one of the coppers of the tetranuclear Cu4S core in a terminal fashion, i.e., using only the oxygen atom. Loss of N2 generates the same my-oxo copper core. The free energies of activation predicted for these two alternative pathways are close to one another and do not provide decisive support for one over the other
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modeling of structure. The residues contributing to the semiocclusion of the T1 copper site are Trp355, Met389, and Met297. There is a negatively charged residue in the neighborhood of the T1 site, Glu296
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C165G
-
Cys165 is not available for Cu cooordination; retaines catalytic activity
C622D
-
no activity, distorted CuA-centre
E296Q
-
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
M297A
-
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
M389A
-
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
W355A
-
mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type
additional information
-
deletion mutant USDA110DELTAnosZ shows no N2O reductase activity
additional information
Bradyrhizobium japonicum USDA110
-
deletion mutant USDA110DELTAnosZ shows no N2O reductase activity
-
additional information
-
strains with a nosXnirX double mutation or nirX single mutation show loss of N2O respiration
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
degradation
-
plays a critical enviromental role in preventing release into the atmosphere of the potent greenhouse gas nitrous oxide
agriculture
P19573
expression of both the senzyme-coding gene nosZ and the mega-cassette of five coding sequences nosFLZDY in Nicotiana tabacum leads to active recombinant N2OR. Extracts from both types of transgenic plants exhibit N2O-reducing activity. The single-gene strategy produces higher reductase capability than the whole-operon approach. Bacterial nitrous oxide reductase expressed in plants could convert N2O into inert N2 without involvement of other Nos proteins
degradation
-
plays a critical enviromental role in preventing release into the atmosphere of the potent greenhouse gas nitrous oxide
agriculture
Pseudomonas stutzeri ATCC 14405
-
expression of both the senzyme-coding gene nosZ and the mega-cassette of five coding sequences nosFLZDY in Nicotiana tabacum leads to active recombinant N2OR. Extracts from both types of transgenic plants exhibit N2O-reducing activity. The single-gene strategy produces higher reductase capability than the whole-operon approach. Bacterial nitrous oxide reductase expressed in plants could convert N2O into inert N2 without involvement of other Nos proteins
-