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Information on EC 1.7.2.6 - hydroxylamine dehydrogenase and Organism(s) Nitrosomonas europaea and UniProt Accession Q50925
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1.7.2.6 hydroxylamine dehydrogenaseIUBMB Comments
The enzymes from the nitrifying bacterium Nitrosomonas europaea [1,4] and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins with seven c-type hemes and one specialized P-460-type heme per subunit. The enzyme converts hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate . While nitrite is the main product, the enzyme from Nitrosomonas europaea can also produce nitric oxide by catalysing the activity of EC 1.7.2.9, hydroxylamine oxidase .
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Word Map
- 1.7.2.6
- ammonia
- monooxygenase
-
nitrification
-
metagenomic
-
nitrify
- nitrospira
- europaea
- no2
- nitrosomonas
-
comammox
- phenylhydrazine
-
ammonium-oxidizing
-
genome-centric
- analysis
The taxonomic range for the selected organisms is: Nitrosomonas europaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
hydroxylamine dehydrogenase, nehao, nohao, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HAO
-
-
hydroxylamine oxidoreductase
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
hydroxylamine:ferricytochrome-c oxidoreductase (nitrite-forming)
The enzymes from the nitrifying bacterium Nitrosomonas europaea [1,4] and the methylotrophic bacterium Methylococcus capsulatus [5] are hemoproteins with seven c-type hemes and one specialized P-460-type heme per subunit. The enzyme converts hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate [3]. While nitrite is the main product, the enzyme from Nitrosomonas europaea can also produce nitric oxide by catalysing the activity of EC 1.7.2.9, hydroxylamine oxidase [2].
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
hydroxylamine + 3 ferricytochrome c
nitric oxide + 3 ferrocytochrome c + 3 H+
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
?
hydrazine + phenazine methosulfate
N2 + reduced phenazine methosulfate
-
-
-
?
hydroxylamine + 2,6-dichlorophenolindophenol
nitric oxide + oxidized 2,6-dichlorophenolindophenol + H+
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
nitrite + ?
-
-
-
-
?
hydroxylamine + cytochrome c
nitric oxide + oxidized cytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricyanide
nitrite + ferrocyanide + H+
-
more than 90% of added hydroxylamine is oxidized to nitrite within 10 min when 10times as much ferricyanide as hydroxylamine is added
-
-
?
hydroxylamine + ferricytochrome c554
nitric oxide + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
-
-
-
-
r
hydroxylamine + N,N'-bis(carboxymethyl)-N,N'-dinitroso-1,4-phenylenediamine
nitric oxide + ?
-
-
-
-
?
hydroxylamine + O2
nitrite + H2O
-
phenazine methosulfate, dichlorophenolindophenol, mammalian cytochrome c and 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium chloride can serve as electron acceptors
-
?
hydroxylamine + phenazine methosulfate
nitric oxide + oxidized phenazine methosulfate + H+
-
-
-
-
?
hydroxylamine + reduced methyl viologen + H+
NH4+ + oxidized methyl viologen + H2O
-
-
-
-
ir
hydroxylamine + Ru(NH3)63+ + H+
nitric oxide + Ru(NH3)62+ + H+
-
-
-
-
ir
nitrite + reduced methyl viologen + H+
NH4+ + oxidized methyl viologen + H2O
-
HAO acts like a cytochrome c nitrite reductase, which catalyzes the six-electron reduction of nitrite to NH4+ by reduced methyl viologen
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
usage of horse heart cytochrome c
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
394315, 394318, 394321, 394323, 394329, 394334, 639387, 656327, 657688, 657690, 657930, 658900, 658903, 696882, 710728, 719635
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
ir
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
in presence of diethyldithiocarbamate, hydroxylamine is oxidized to nitrite, for each mol of nitrite produced approximately 1 mol of diethyldithiocarbamate is oxidized to bis(diethyldithiocarbamoyl)disulfide
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
Nitrosomonas cytochrome c-554 can act as electron carrier
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
mammalian cytochrome c can serve as electron acceptor
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
energy production
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
ferricytochrome is a c554 better electron acceptor than horse heart cytochrome c
-
-
?
additional information
?
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
-
HAO does not catalyze the disproportionation of hydroxylamine, despite the thermodynamic favorability of such a process, and the apparent opportunity presented by the HAO structure
-
-
?
additional information
?
-
-
oxidation of hydroxylamine by the enzyme results in the production of a mixture of HNO2/HNO3
-
-
?
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
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
ir
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
energy production
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
the enzyme contains 24 hemes, localized in four clusters within each monomer
heme
-
-
heme
-
each alpha,beta subunit of the (alpha,beta)3 subunit structure contains 7-8 c-type hemes and one prosthetic group P-460, P-460 is a MW 17000 protein fragment
heme
-
resolution of the hemes by redox potentiometry and electron spin resonance spectroscopy
heme
-
enzyme consists of one alpha-beta-3 subunit and contains seven-eight c-type hemes and P460
heme
-
8 hemes per subunit: a triheme cluster, four hemes that are electronically coupled in two distinguishable pairs and one of these pairs is at the active site, and one heme that is not part of a cluster
heme
-
multi-heme enzyme containing at least 5 thermodynamically distinct c-type hemes and the heme-like moiety P460
heme
-
resolution of multiple heme centers by electron paramagnetic resonance spectroscopy
heme
-
contains hemes c-553, c-559 and P-460 in the ratio 5:2:1, P-460 is the site of electron entry
heme
-
each subunit of the enzyme contains 7 c-hemes and 1 heme P460. The latter, a c-heme crosslinked from a methylene carbon to the ring of a protein tyrosine, forms part of the active site
heme
-
contains seven C-type hemes and one P460-type heme per alphabeta subunit
heme
-
each subunit contains eight c-type hemes (inclusive one P460 heme)
heme
-
each subunit contains seven c-type hemes and an eighth heme known as P460
heme
-
the enzyme contains eight hemes per subunit, seven C-type cytochromes and one heme P460
additional information
-
each monomer contains 7 c-type hemes and a novel heme known as P460, the role of the c-hemes appears to be the transfer of electrons from the P460 active site to 1 or more electron acceptors, cytochrome c554 is the most likely candidate as the electron acceptor
-
additional information
-
hydroxylamine oxidation takes place on three novel hemes known as P460
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ce(NH4)2(NO3)6
-
0.1 mM, stimulates the rate of oxidation of NH2OH 2.6-fold and inhibits production of HNO2 by 40%
Fe
Mn2+
-
0.001 mM, stimulation of NH2OH utilization, stimulation at pH 6 and pH 9 is approximately 40% greater than at pH 7 and pH 8
additional information
-
the presence of Mn2+ results in decreased formation of NO and increased formation of N2O
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylhydrazine
an HAO enzyme specific inhibitor, inhibits about 60% of enzyme NeHAO activity at 0.01 mM
Cd2+
-
decreases in hydroxylamine oxidoreductase-specific oxygen uptake rate followed by a recovery of hydroxylamine oxidoreductase-specific oxygen uptake rate above steady-state levels do occur upon exposure to Cd2+ concentrations of 0.03 mM and greater
Ce(NH4)2(NO3)6
-
0.1 mM, stimulates the rate of oxidation of NH2OH 2.6-fold and inhibits production of HNO2 by 40%
Mn2+
-
complete inhibition of the oxidation of HNO to NO at 0.001 mM, inhibition of HNO2 synthesis is the same at pH 6,7,8 and 9
additional information
no significant changes in the NeHAO and NoHAO activities by addition of 0.5% DMSO and 0.01% Triton X-100
-
additional information
-
no significant changes in the NeHAO and NoHAO activities by addition of 0.5% DMSO and 0.01% Triton X-100
-
additional information
-
hydroxylamine oxidoreductase-specific oxygen uptake rates are not adversely affected at Cd2+ concentrations up to 0.02 mM
-
additional information
-
in the presence of Ru(NH3)2+ and Ru(NH3)3+ at ratios exceeding 200:1, HAO exhibits no detectable Ru(NH3)2+-NO2- oxidoreductase activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no significant changes in the NeHAO and NoHAO activities by addition of 0.5% DMSO and 0.01% Triton X-100
-
additional information
-
no significant changes in the NeHAO and NoHAO activities by addition of 0.5% DMSO and 0.01% Triton X-100
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
ferricytochrome c
-
from Rhodospirillum rubrum, Saccharomyces oviformis and cow
0.04
ferricytochrome c
-
from Chlorobium limicola forma sp. thiosulfatophilum
0.003
hydrazine
-
pH 7.5, 25°C, with enzyme form HAO-A, that forms only the monocyano derivative of heme P460
0.005
hydrazine
-
pH 7.5, 25°C, with enzyme form HAO-B, that forms a mono- and dicyano complex
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
overview: effect of pH on rate of reduction of heme c553 of the enzyme by NH2OH, rate constant for reduction of hemes of the enzyme by dithionite at 2°C and 19°C and by NH2OH or NH2NH2 at 2°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
-
crude lysate, in 0.1 M sodium glycine buffer at pH 8.8, temperature not specified in the publication
0.6
-
after 60fold purification, in 0.1 M sodium glycine buffer at pH 8.8, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
-
rate of reduction of hemes c 553 of the enzyme increases with pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
changes in enzyme conformation imposed by changes in solvent, temperature or pressure affect the rates of intramolecular electron transfer from the substrate site to c hemes
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
no single copy of hao is essential to the cell
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
-
3 * 63000 + 3 * 11000, (alpha,beta)3 subunit structure, SDS-PAGE, 200000 MW enzyme forms a 63000 MW monomer after heme removal, hydroxylamine oxidoreductase probably consists of 3 molecules of monoheme c-type cytochrome with a MW of 11000 and 3 tightly complexed molecules of a catalytically active MW 63000 protein containing 6 c-type hemes and one P-460 heme, SDS-PAGE
140000
200000
63000
63000
-
3 * 63000 + 3 * 11000, (alpha,beta)3 subunit structure, SDS-PAGE, 200000 MW enzyme forms a 63000 MW monomer after heme removal, hydroxylamine oxidoreductase probably consists of 3 molecules of monoheme c-type cytochrome with a MW of 11000 and 3 tightly complexed molecules of a catalytically active MW 63000 protein containing 6 c-type hemes and one P-460 heme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
hypothesis that the enzyme is functionally a dimer in which electrons rapidly equilibrate between the c-hemes of each subunit but not between oligomers
hexamer
-
3 * 63000 + 3 * 11000, (alpha,beta)3 subunit structure, SDS-PAGE, 200000 MW enzyme forms a 63000 MW monomer after heme removal, hydroxylamine oxidoreductase probably consists of 3 molecules of monoheme c-type cytochrome with a MW of 11000 and 3 tightly complexed molecules of a catalytically active MW 63000 protein containing 6 c-type hemes and one P-460 heme, SDS-PAGE
homotrimer
oligomer
trimer
oligomer
-
alpha2 or alpha3 oligomeric structure with a subunit of 63 kDa, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2.4 M ammonium sulfate, 50 mM Tris-HCL, at pH 8.0
to 2.1 A resolution. Heme P460 contains two covalent cross-links between the porphyrin and a Tyr residue. When purified from source, an unknown physiological HAO binding partner NE1300 is present within the crystal. Protein NE1300 may play a structural role in the ternary complex with cytochrome c554, the physiological electron acceptor of the enzyme
microbatch-under-oil method, using 0.1 M potassium nitrate, 0.1 M MES pH 7.5 and 46% (v/v) PEG 400
-
using 0.1 M potassium nitrate, 0.1 M MES pH 7.5 and 46% (w/v) PEG 400
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutants with only one or two of the three copies of the gene for hydroxylamine oxidoreductase have reduced enzyme activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
changes in enzyme conformation imposed by changes in solvent, temperature or pressure affect the rates of intramolecular electron transfer from the substrate site to c hemes
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
changes in enzyme conformation imposed by changes in solvent, temperature or pressure affect the rates of intramolecular electron transfer from the substrate site to c hemes
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
on exposure to air, the 100% reduced enzyme sample is oxidized within about 1 min
-
394321
the enzyme is inactivated by incubation of 1 mM enzyme with a 5fold excess of peroxide for 1 h. The enzyme is also inactivated in the presence of H2O2
-
719635
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from strain ATCC 19718 by anion exchange chromatography, gel filtration, and hdroxyapatite chromatography
ammonium sulfate precipitation, DEAE cellulose column chromatography, gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration
-
ammonium sulfate precipitation, octyl-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation, Sepharose CL-6B column chromatography, DEAE-Sephacel column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, Sepharose CL-6B column chromatography, DEAE-Sephacel gel filtration, and Sephadex G100 gel filtration
-
ammonium sulfate precipitation, Sepharose CL-6B column chromatography, DEAE-Sephacel gel filtration, octyl Sepharose column chromatography, and Sephadex G-100 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme level remains highly stable during ammonia starvation. The enzyme level shows no significant change when the cells are incubated with 0.2 mM ammonia for 60 min at 4°C or 26°C
-
there is some increase in the enzyme level only after 4 h incubation of starved Nitrosomonas europaea cells with 2 mM ammonia
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
use of hydroxylamine oxidoreductase to differentiate Nitrosomonas spp. and to identify autotrophic ammonia oxidizing bacteria. The ensembled use of single strand confirmation polymorphism and HAO enzyme zymogram in fingerprinting AOB provide better resolution and evenness, contributing significantly in autotrophic ammonia oxidizing bacteria diversity studies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rees, M.K.
Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I. Purification of hydroxylamine oxidase
Biochemistry
7
353-366
1968
Nitrosomonas europaea
Tatsuaki, T.; Yusuke, T.; Reiji, T.
Cloning and expression of the hydroxylamine oxidase gene of Nitrosomonas europaea in Pseudomonas putida
Hakko Kogaku Kaishi
66
103-107
1988
Nitrosomonas europaea
-
Balny, C.; Hooper, A.B.
Effect of solvent, pressure and temperature on reaction rates of the multiheme hydroxylamine oxidoreductase. Evidence for conformational change
Eur. J. Biochem.
176
273-279
1988
Nitrosomonas europaea
Prince, R.C.; Hooper, A.B.
Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and electron spin resonance spectroscopy
Biochemistry
26
970-974
1987
Nitrosomonas europaea
-
Hooper, A.B.; Tran, M.; Balny, C.
Kinetics of reduction by substrate or dithionite and heme-heme electron transfer in the multiheme hydroxylamine oxidoreductase
Eur. J. Biochem.
141
565-571
1984
Nitrosomonas europaea
Hooper, A.B.; Debey, P.; Andersson, K.K.; Balny, C.
Heme P460 of hydroxylamine oxidoreductase of Nitrosomonas. Reaction with CO and H2O2
Eur. J. Biochem.
134
83-87
1983
Nitrosomonas europaea
Lipscomb, J.D.; Hooper, A.B.
Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy
Biochemistry
21
3965-3972
1982
Nitrosomonas europaea
Terry, K.R.; Hooper, A.B.
Hydroxylamine oxidoreductase: a 20-heme, 200 000 molecular weight cytochrome c with unusual denaturation properties which forms a 63 000 molecular weight monomer after heme removal
Biochemistry
20
7026-7032
1981
Nitrosomonas europaea
Hooper, A.B.; Terry, K.R.
Hydroxylamine oxidoreductase of Nitrosomonas. Production of nitric oxide from hydroxylamine
Biochim. Biophys. Acta
571
12-20
1979
Nitrosomonas europaea, Nitrosomonas europaea Schmidt
Yamanaka, T.; Shinra, M.; Takahashi, K.; Shibasaka, M.
Highly purified hydroxylamine oxidoreductase derived from Nitrosomonas europaea. Some physicochemical and enzymatic properties
J. Biochem.
86
1101-1108
1979
Nitrosomonas europaea
Hooper, A.B.; Maxwell, P.C.; Terry, K.R.
Hydroxylamine oxidoreductase from Nitrosomonas: absorption spectra and content of heme and metal
Biochemistry
17
2984-2989
1978
Nitrosomonas europaea
Hooper, A.B.; Terry, K.R.; Maxwell, P.C.
Hydroxylamine oxidoreductase of Nitrosomonas. Oxidation of diethyldithiocarbamate concomitant with stimulation of nitrite synthesis
Biochim. Biophys. Acta
462
141-152
1977
Nitrosomonas europaea
Andersson, K.K.; Kent, T.A.; Lipscomb, J.D.; Hooper, A.B.; Munck, E.
Mossbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting
J. Biol. Chem.
259
6833-6840
1984
Nitrosomonas europaea
Rees, M.K.
Studies on the hydroxylamine metabolism of Nitrosomonas europaea. II. Molecular properties of the electron-transport particle, hydroxylamine oxidase
Biochemistry
7
366-372
1968
Nitrosomonas europaea
Ritchie, G.A.F.; Nicholas, D.J.D.
The partial characterization of purified nitrite reductase and hydroxylamine oxidase from Nitrosomonas europaea
Biochem. J.
138
471-480
1974
Nitrosomonas europaea
Nasri, H.; Fischer, J.; Weiss, R.
Synthesis and characterization of five-coordinate high-spin iron(II) porphyrin complexes with unusually large quadrupole splittings. Models for the P460 center of hydroxylamine oxidoreductase from Nitrosomonas
J. Am. Chem. Soc.
109
2549-2550
1987
Nitrosomonas europaea
-
Numata, M.; Saito, T.; Yamazaki, Y.; Yamanaka, T.
Cytochrome p-460 of Nitrosomonas europaea: further purification and further characterization
J. Biochem.
108
1016-1021
1990
Nitrosomonas europaea
Hooper, A.B.; Balny, C.
Reaction of oxygen with hydroxylamine oxidoreductase of Nitrosomonas
FEBS Lett.
144
299-303
1982
Nitrosomonas europaea, Nitrosomonas sp.
Yamanaka, T.; Sakano, Y.
Oxidation of hydroxylamine to nitrite catalyzed by hydroxylamine oxidoreductase purified from Nitrosomonas europaea
Curr. Microbiol.
4
239-244
1980
Nitrosomonas europaea
-
Arciero, D.M.; Golombek, A.; Hendrich, M.P.; Hooper, A.B.
Correlation of optical and EPR signals with the P460 heme of hydroxylamine oxidoreductase from Nitrosomonas europaea
Biochemistry
37
523-529
1998
Nitrosomonas europaea
Arciero, D.M.; Hooper, A.B.
Hydroxylamine oxidoreductase from Nitrosomonas europaea is a multimer of an octa-heme subunit
J. Biol. Chem.
268
14645-14654
1993
Nitrosomonas europaea
Collins, M.J.; Arciero, D.M.; Hooper, A.B.
Optical spectropotentiometric resolution of the hemes of hydroxylamine oxidoreductase. Heme quantitation and pH dependence of Em
J. Biol. Chem.
268
14655-14662
1993
Nitrosomonas europaea
Hendrich, M.P.; Petasis, D.; Arciero, D.M.; Hooper, A.B.
Correlations of structure and electronic properties from EPR spectroscopy of hydroxylamine oxidoreductase
J. Am. Chem. Soc.
123
2997-3005
2001
Nitrosomonas europaea
Hommes, N.G.; Sayavedra-Soto, L.A.; Arp, D.J.
Mutagenesis of hydroxylamine oxidoreductase in Nitrosomonas europaea by transformation and recombination
J. Bacteriol.
178
3710-3714
1996
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19178
Logan, M.S.P.; Hooper, A.B.
Suicide Inactivation of Hydroxylamine Oxidoreductase of Nitrosomonas europaea by Organohydrazines
Biochemistry
34
9257-9264
1995
Nitrosomonas europaea
Nejidat, A.; Shmuely, H.; Abeliovich, A.
Effect of ammonia starvation on hydroxylamine oxidoreductase activity of Nitrosomonas europaea
J. Biochem.
121
957-960
1997
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Yamagata, A.; Hirota, R.; Kato, J.; Kuroda, A.; Ikeda, T.; Takiguchi, N.; Ohtake, H.
Mutational analysis of the multicopy hao gene coding for hydroxylamine oxidoreductase in Nitrosomonas sp. strain ENI-11
Biosci. Biotechnol. Biochem.
64
1754-1757
2000
Nitrosomonas europaea, Nitrosomonas europaea ENI-11, Nitrosomonas sp., Nitrosomonas sp. ENI-11
DiSpirito, A.; Taaffe, L.R.; Lipscomb, J.D.; Hooper, A.B.
A 'blue' copper oxidase from Nitrosomonas europaea
Biochim. Biophys. Acta
827
320-326
1985
Nitrosomonas europaea
-
Logan, M.S.P.; Balny, C.; Hooper, A.B.
Reaction with cyanide of hydroxylamine oxidoreductase of Nitrosomonas europaea
Biochemistry
34
9028-9037
1995
Nitrosomonas europaea
Tokuyama, T.; Mine, A.; Kamiyama, K.; Yabe, R.; Satoh, K.; Matsumoto, H.; Takahashi, R.; Itonaga, K.
Nitrosomonas communis strain YNSRA, an ammonia-oxidizing bacterium, isolated from the reed rhizoplane in an aquaponics plant
J. Biosci. Bioeng.
98
309-312
2004
Nitrosomonas communis, Nitrosomonas communis YNSRA, Nitrosomonas europaea, Nitrosomonas sp. K1
Arp, D.J.; Sayavedra-Soto, L.A.; Hommes, N.G.
Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea
Arch. Microbiol.
178
250-255
2002
Nitrosomonas europaea
Hommes, N.G.; Sayavedra-Soto, L.A.; Arp, D.J.
The roles of the three gene copies encoding hydroxylamine oxidoreductase in Nitrosomonas europaea
Arch. Microbiol.
178
471-476
2002
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Hendrich, M.P.; Upadhyay, A.K.; Riga, J.; Arciero, D.M.; Hooper, A.B.
Spectroscopic characterization of the NO adduct of hydroxylamine oxidoreductase
Biochemistry
41
4603-4611
2002
Nitrosomonas europaea
Cabail, M.Z.; Pacheco, A.A.
Selective one-electron reduction of Nitrosomonas europaea hydroxylamine oxidoreductase with nitric oxide
Inorg. Chem.
42
270-272
2003
Nitrosomonas europaea
Cabail, M.Z.; Kostera, J.; Pacheco, A.A.
Laser photoinitiated nitrosylation of 3-electron reduced Nm europaea hydroxylamine oxidoreductase: kinetic and thermodynamic properties of the nitrosylated enzyme
Inorg. Chem.
44
225-231
2005
Nitrosomonas europaea
Kurnikov, I.V.; Ratner, M.A.; Pacheco, A.A.
Redox equilibria in hydroxylamine oxidoreductase. Electrostatic control of electron redistribution in multielectron oxidative processes
Biochemistry
44
1856-1863
2005
Nitrosomonas europaea
Pulcu, G.S.; Elmore, B.L.; Arciero, D.M.; Hooper, A.B.; Elliott, S.J.
Direct electrochemistry of tetraheme cytochrome c(554) from Nitrosomonas europaea: redox cooperativity and gating
J. Am. Chem. Soc.
129
1838-1839
2007
Nitrosomonas europaea
Radniecki, T.S.; Semprini, L.; Dolan, M.E.
Expression of merA, trxA, amoA, and hao in continuously cultured Nitrosomonas europaea cells exposed to cadmium sulfate additions
Biotechnol. Bioeng.
104
1004-1011
2009
Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718
Cedervall, P.E.; Hooper, A.B.; Wilmot, C.M.
Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea
Acta Crystallogr. Sect. F
65
1296-1298
2009
Nitrosomonas europaea
Kostera, J.; McGarry, J.; Pacheco, A.
Enzymatic interconversion of ammonia and nitrite: The right tool for the job
Biochemistry
49
8546-8553
2010
Nitrosomonas europaea
Hooper, A.
Spectroscopic and rapid kinetic studies of reduction of cytochrome c554 by hydroxylamine oxidoreductase from Nitrosomonas europaea
Biochemistry
30
11466-11472
1991
Nitrosomonas europaea
Hendrich, M.; Logan, M.; Andersson, K.; Arciero, D.; Lipscomb, J.; Hooper, A.
The active site of hydroxylamine oxidoreductase from Nitrosomonas: Evidence for a new metal cluster in enzymes
J. Am. Chem. Soc.
116
11961-11968
1994
Nitrosomonas europaea, Nitrosomonas europaea Schmidt
-
Igarashi, N.; Moriyama, H.; Fujiwara, T.; Fukumori, Y.; Tanaka, N.
The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
Nat. Struct. Biol.
4
276-284
1997
Nitrosomonas europaea (Q50925)
Cedervall, P.; Hooper, A.B.; Wilmot, C.M.
Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner
Biochemistry
52
6211-6218
2013
Nitrosomonas europaea (Q50925), Nitrosomonas europaea ATCC 19718 (Q50925)
Keluskar, R.; Desai, A.
Evaluation of hydroxylamine oxidoreductase as a functional and phylogenetic marker to differentiate Nitrosomonas spp
J. Basic Microbiol.
54
261-268
2013
Nitrosomonas europaea
Nishigaya, Y.; Fujimoto, Z.; Yamazaki, T.
Optimized inhibition assays reveal different inhibitory responses of hydroxylamine oxidoreductases from beta- and gamma-proteobacterial ammonium-oxidizing bacteria
Biochem. Biophys. Res. Commun.
476
127-133
2016
Nitrosococcus oceani, Nitrosococcus oceani ATCC 19707, Nitrosomonas europaea (Q50925), Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718 (Q50925), Nitrosomonas sp. JPCCT2, Nitrosospira multiformis
Smith, M.A.; Majer, S.H.; Vilbert, A.C.; Lancaster, K.M.
Controlling a burn outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460
Chem. Sci.
10
3756-3764
2019
Nitrosomonas europaea (Q50925)
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