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Information on EC 1.7.2.4 - nitrous-oxide reductase and Organism(s) Achromobacter cycloclastes and UniProt Accession P94127
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1.7.2.4 nitrous-oxide reductaseIUBMB Comments
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.
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Word Map
- 1.7.2.4
-
denitrification
-
denitrify
- nitrite
-
greenhouse
- denitrificans
- paracoccus
- stutzeri
-
dinitrogen
-
wastewater
-
binuclear
-
tetranuclear
- cycloclastes
-
mixed-valence
-
multicopper
-
ammonia-oxidizing
-
n-cycle
- nautica
-
wolinella
-
arable
- nitrospirae
-
stratospheric
- agriculture
-
t-rflp
- degradation
The taxonomic range for the selected organisms is: Achromobacter cycloclastes
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
nitrous oxide reductase, n2o reductase, n(2)or, nitrous-oxide reductase, cnosz, hdn2or, psn2or, z-type n2or, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N(2)OR
-
-
-
-
N2O reductase
nitrous oxide reductase
N2O reductase
-
-
-
-
nitrous oxide reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
55576-44-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N2O + reduced benzyl viologen
N2 + oxidized benzyl viologen
-
-
-
?
N2O + reduced pseudoazurin
N2 + oxidized pseudoazurin
blue copper electron-transfer protein pseudoazurin is capable of mediating electron transfer to the nitrous oxide reductase. Pseudoazurin binds near copper site CuA, with parameters consistent with the formation of a transient, weakly-bound complex. Pseudoazurin a strong candidate for the physiological electron donor to th enzyme
-
-
?
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
-
-
-
?
N2O + reduced benzyl viologen
N2 + H2O + benzyl viologen
-
-
-
-
?
N2O + reduced methyl viologen
N2 + H2O + methyl viologen
-
-
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
-
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
under some conditions, electron transfer may be rate limiting in N2O reduction. The transition state is stabilized by H-bonding interactions between the active site and an N2O-derived intermediate bound to the catalytic CuZ cluster
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
methyl viologen as electron donor
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N2O + reduced pseudoazurin
N2 + oxidized pseudoazurin
blue copper electron-transfer protein pseudoazurin is capable of mediating electron transfer to the nitrous oxide reductase. Pseudoazurin binds near copper site CuA, with parameters consistent with the formation of a transient, weakly-bound complex. Pseudoazurin a strong candidate for the physiological electron donor to th enzyme
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
-
-
-
?
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
copper
-
the fully reduced all-Cu(I) state of CuZ is the catalytically relevant redox state of N2OR
Cu
Cu2+
a copper enzyme, conformational changes of the CuA center may affect electron transfer from the physiological electron donor and the electron-transfer rate from CuA to CuZ, overview
Cu2+
a copper enzyme, two copper centers, CuA and CuB, per monomer, binding structure, detailed analysis of the pH effect at the CuZ site, e.g. using spectroscopic and computational methods, overview
Cu2+
the enzyme contains average 4.5 Cu and 1.2 S per monomer
Cu
-
Cu is bound by apo NosL, a coexpressed protein which is necessary for the assembling process of nitrous oxide reductase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S2O42-
-
irreversible formation of inactive blue form of the enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0191
N2O
pH 7.1, temperature not specified in the publication
0.0138
reduced benzyl viologen
pH 7.1, temperature not specified in the publication
0.0288
reduced pseudoazurin
pH 7.1, temperature not specified in the publication
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
steady-state kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.1
assayed in the standard dithionite methyl viologen assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7 - 10.6
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NOSZ_ACHCY
642
1
70922
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
perturbations of the protein conformation induced by pH variations, although the principal secondary structure elements are largely unaltered
additional information
-
perturbations of the protein conformation induced by pH variations, although the principal secondary structure elements are largely unaltered
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anaerobical purification of N2OR under an Ar atmosphere by three different steps of anion exchange chromatography, followed by cytochrome c affinity chromatography and ultrafiltration
DEAE cellulose column chromatography, hydroxyapatite column chromatography, Mono Q10 anion-exchange column chromatography, and Sephadex S-200 gel filtration
DEAE-FF ion exchange chromatography and Resource Q column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the gene encoding the enzyme in the nos cluster is cloned from a genomic library
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hulse, C.L.; Averill, B.A.
Isolation of a high specific activity pink, monomeric nitrous oxide reductase from Achromobacter cycloclastes
Biochem. Biophys. Res. Commun.
166
729-735
1990
Achromobacter cycloclastes
Chan, J.M.; Bollinger, J.A.; Grewell, C.L.; Dooley, D.M.
Reductively activated nitrous oxide reductase reacts directly with Substrate
J. Am. Chem. Soc.
126
3030-3031
2004
Achromobacter cycloclastes
Henry, S.; Bru, D.; Stres, B.; Hallet, S.; Philippot, L.
Quantitative detection of the nosZ gene, encoding nitrous oxide reductase, and comparison of the abundances of 16S rRNA, narG, nirK, and nosZ genes in soils
Appl. Environ. Microbiol.
72
5181-5189
2006
Achromobacter cycloclastes, Alcaligenes faecalis, Bradyrhizobium japonicum, Pseudomonas denitrificans (nom. rej.), Sinorhizobium meliloti, Hyphomicrobium denitrificans, Ensifer adhaerens, Pseudomonas fluorescens (Q9F0W4), Pseudomonas denitrificans (nom. rej.) CCUG 2519, Pseudomonas fluorescens C7R12 (Q9F0W4), Sinorhizobium meliloti 50, Ensifer adhaerens SN611
Taubner, L.M.; McGuirl, M.A.; Dooley, D.M.; Copie, V.
Structural studies of Apo NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein
Biochemistry
45
12240-12252
2006
Achromobacter cycloclastes
Paraskevopoulos, K.; Antonyuk, S.V.; Sawers, R.G.; Eady, R.R.; Hasnain, S.S.
Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastes
J. Mol. Biol.
362
55-65
2006
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes, Achromobacter cycloclastes 1013 (P94127)
Fujita, K.; Dooley, D.M.
Insights into the mechanism of N2O reduction by reductively activated N2O reductase from kinetics and spectroscopic studies of pH effects
Inorg. Chem.
46
613-615
2007
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes
Ghosh, S.; Gorelsky, S.I.; George, S.D.; Chan, J.M.; Cabrito, I.; Dooley, D.M.; Moura, J.J.; Moura, I.; Solomon, E.I.
Spectroscopic, computational, and kinetic studies of the mu4-sulfide-bridged tetranuclear CuZ cluster in N2O reductase: pH effect on the edge ligand and its contribution to reactivity
J. Am. Chem. Soc.
129
3955-3965
2007
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes, Marinobacter nauticus (Q19Q69)
Fujita, K.; Chan, J.M.; Bollinger, J.A.; Alvarez, M.L.; Dooley, D.M.
Anaerobic purification, characterization and preliminary mechanistic study of recombinant nitrous oxide reductase from Achromobacter cycloclastes
J. Inorg. Biochem.
101
1836-1844
2007
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes, Achromobacter cycloclastes IAM1013 (P94127)
Fujita, K.; Hirasawa-Fujita, M.; Brown, D.E.; Obara, Y.; Ijima, F.; Kohzuma, T.; Dooley, D.M.
Direct electron transfer from pseudoazurin to nitrous oxide reductase in catalytic N2O reduction
J. Inorg. Biochem.
115
163-173
2012
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes
EXTERNAL LINKS (specific for EC-Number 1.7.2.4)
Transporter Classification Database (TCDB): 3.D.4.2.2
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