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Information on EC 1.7.2.4 - nitrous-oxide reductase and Organism(s) Pseudomonas stutzeri and UniProt Accession P19573

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IUBMB 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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Pseudomonas stutzeri
UNIPROT: P19573
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The taxonomic range for the selected organisms is: Pseudomonas stutzeri
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
nitrous oxide reductase, n2o reductase, n(2)or, nitrous-oxide reductase, cnosz, hdn2or, z-type n2or, psn2or, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N(2)OR
-
-
-
-
N2O reductase
-
-
-
-
nitrous oxide reductase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
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 hide
55576-44-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N2O + reduced methyl viologen
N2 + oxidized methyl viologen
show the reaction diagram
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
-
dependent on. The enzyme nitrous oxide reductase contains two copper sites: a binuclear site known as CuA that functions as an electron transfer site, and an unusual tetranuclear copper sulfide cluster active site, where N2O binds and is reduced. Two forms of this tetranuclear site have been structurally characterized. One, known as CuZ*, has a mu4 sulfide ligand bridging all four coppers and a solvent derived ligand on an open edge (the CuI-CuIV edge) where N2O is proposed to bind. The other form of the cluster, known as CuZ, has an additional mu2 sulfur ligand bridging the CuI-CuIV edge. Raman spectroscopic analysis and computationa modelling of Cu site structure and mechanism, binding and interaction, overview. Protonation state of the mu2 sulfur ligand on the CuI-CuIV edge in 1-hole and 2-hole CuZ
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S2O42-
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irreversible formation of inactive blue form of the enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
453
enzyme purified from transgenic Nicotiana tabacum, pH 7.1, 37°C
5.5
-
wild-type
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NOSZ_PSEST
638
1
70822
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
118000
-
gel filtration
120000
-
gel filtration
130000
-
non denaturating PAGE
62000
-
alpha2, 2 * 62000, SDS-PAGE
74000
-
2 * 74000, SDS-PAGE
87000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C165G
C622D
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no activity, distorted CuA-centre
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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85% inactivation after 20 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a pink form is isolated when the purification is done aerobically, a purple form when the purification is under anaerobic conditions
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Nicotiana tabacum
expression in Escherichia coli HB101, no activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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
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plays a critical enviromental role in preventing release into the atmosphere of the potent greenhouse gas nitrous oxide
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rasmussen, T.; Berks, B.C.; Sanders-Loehr, J.; Dooley, D.M.; Zumft, W.G.; Thomson, A.J.
The catalytic center in nitrous oxide reductase, CuZ, is a copper-sulfide cluster
Biochemistry
39
12753-12756
2000
Paracoccus pantotrophus, Pseudomonas stutzeri
Manually annotated by BRENDA team
Farrar, J.A.; Zumft, W.G.; Thomson, A.J.
CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase
Proc. Natl. Acad. Sci. USA
95
9891-9896
1998
Pseudomonas stutzeri
Manually annotated by BRENDA team
Dreusch, A.; Riester, J.; Kroneck, P.M.; Zumft, W.G.
Mutation of the conserved Cys165 outside of the CuA domain destabilizes nitrous oxide reductase but maintains its catalytic activity. Evidence for disulfide bridges and a putative protein disulfide isomerase gene
Eur. J. Biochem.
237
447-453
1996
Pseudomonas stutzeri
Manually annotated by BRENDA team
Viebrock, A.; Zumft, W.G.
Molecular cloning, heterologous expression, and primary structure of the structural gene for the copper enzyme nitrous oxide reductase from denitrifying Pseudomonas stutzeri
J. Bacteriol.
170
4658-4668
1988
Pseudomonas stutzeri
Manually annotated by BRENDA team
Coyle, C.L.; Zumft, W.G.; Kroneck, P.M.H.; Krner, H.; Jakob, W.
Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme
Eur. J. Biochem.
153
459-467
1985
Pseudomonas stutzeri
Manually annotated by BRENDA team
Snyder, S.W.; Hollocher, T.C.
Nitrous oxide reductase and the 120,000 MW copper protein of N2-producing denitrifying bacteria are different entities
Biochem. Biophys. Res. Commun.
119
588-592
1984
Paracoccus denitrificans, Pseudomonas denitrificans (nom. rej.), Pseudomonas stutzeri
Manually annotated by BRENDA team
Zumft, W.G.; Matsubara, T.
A novel kind of multi-copper protein as terminal oxidoreductase of nitrous oxide respiration in Pseudomonas perfectomarinus
FEBS Lett.
148
107-112
1982
Pseudomonas stutzeri
-
Manually annotated by BRENDA team
Wan, S.; Mottiar, Y.; Johnson, A.M.; Goto, K.; Altosaar, I.
Expression of the nos operon proteins from Pseudomonas stutzeri in transgenic plants to assemble nitrous oxide reductase
Transgenic Res.
21
593-603
2012
Pseudomonas stutzeri (P19573), Pseudomonas stutzeri, Pseudomonas stutzeri ATCC 14405 (P19573)
Manually annotated by BRENDA team
Johnston, E.M.; DellAcqua, S.; Pauleta, S.R.; Moura, I.; Solomon, E.I.
Protonation state of the Cu4S2 CuZ site in nitrous oxide reductase redox dependence and insight into reactivity
Chem. Sci.
6
5670-5679
2015
Paracoccus pantotrophus, Pseudomonas stutzeri
Manually annotated by BRENDA team