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ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
-
-
-
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
mechanism
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
ping pong kinetic mechanism
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
Asp402 acts as the active site base of the enzyme, mechanism, substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
Asp402 acts as the active site base of the enzyme, mechanism: catalysis is initiated by the active site base Asp402 that deprotonates the neutral substrate to yield a carbanion that can attack the N-5 position of the oxidized flavin, CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
detailed mechanism, with carbanion reaction intermediate formation, an aspartate residue is the active site base, substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane, the active site of the enzyme is a hydrophobic channel, tunneling, overview
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
mechanism, involves removal of a proton from the nitroalkane, forming a carbanion which adds to the N5 of the flavin, elimination of nitrite from the resulting adduct forms an electrophilic imine intermediate which can be attacked by hydroxide
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
mechanism, transition-state stabilization is essential, protein-substrate interactions in the transition state, reaction involves quantum mechaniscal tunneling, Asp402 is involved in initial abstraction of a proton from the neutral substrate, overview
-
ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O
critical importance of the interaction between Asp402 and Arg409 for proton abstraction by nitroalkane oxidase
-
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1-nitroalkane + O2 + H2O
aldehyde + H2O2 + nitrite
-
-
-
-
?
1-nitrobutane + H2O + O2
butyraldehyde + nitrite + H2O2
-
-
-
-
?
1-nitrobutane + O2
butyraldehyde + HNO2
-
-
-
-
?
1-nitrobutane + O2 + H2O
butyraldehyde + nitrite + H2O2
1-nitrohexane + H2O + O2
?
-
-
-
?
1-nitrohexane + O2
hexanaldehyde + HNO2
-
-
-
-
?
1-nitrohexane + O2 + H2O
hexanal + nitrite + H2O2
1-nitrohexane + O2 + H2O
hexanaldehyde + nitrite + H2O2
-
-
-
-
?
1-nitrooctane + H2O + O2
?
-
-
-
?
1-nitrooctane + O2 + H2O
octanal + nitrite + H2O2
-
-
-
?
1-nitropentane + O2
pentanaldehyde + HNO2
-
-
-
-
?
1-nitropropane + H2O
propanal + nitrite + H2O2
-
-
-
?
1-nitropropane + H2O + O2
propionaldehyde + nitrite + H2O2
1-nitropropane + O2
propionaldehyde + HNO2
-
-
-
-
?
2-nitropropane + H2O
propanone + nitrite + H2O2
-
-
-
?
2-nitropropane + H2O + O2
acetone + nitrite + H2O2
2-nitropropane + O2
acetone + HNO2
-
-
-
-
?
2-nitropropane + O2
acetone + nitrite
-
-
-
-
?
3-nitropropanoic acid + H2O + O2
2-oxopropanoic acid + nitrite + H2O2
-
-
-
-
?
benzoate + H2O + O2
?
-
-
-
-
r
nitroalkane + O2 + H2O
aldehyde or ketone + nitrite + H2O2
-
neutral nitroalkanes
-
-
?
nitroethane + H2O
acetaldehyde + nitrite + H2O2
-
-
-
-
?
nitroethane + H2O
ethanal + nitrite + H2O2
nitroethane + H2O + O2
?
-
-
-
-
?
nitroethane + H2O + O2
acetaldehyde + nitrite + H2O2
nitroethane + H2O + O2
ethanal + nitrite + H2O2
-
-
-
?
nitroethane + O2
acetaldehyde + HNO2
nitroethane + O2 + H2O
acetaldehyde + nitrite + H2O2
-
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
nitroethane + O2 + H2O
ethanal + nitrite + H2O2 + H+
phenylacetic acid + H2O + O2
?
-
-
-
-
r
phenylnitromethane + O2
benzaldehyde + HNO2
-
-
-
-
?
phenylnitromethane + O2 + H2O
? + nitrite + H2O2
-
-
-
-
?
phenylnitromethane + O2 + H2O
phenylaldehyde + nitrite + H2O2
-
-
-
-
?
additional information
?
-
1-nitrobutane + O2 + H2O
butyraldehyde + nitrite + H2O2
-
-
-
-
?
1-nitrobutane + O2 + H2O
butyraldehyde + nitrite + H2O2
-
400fold more effective than nitroethane
-
-
?
1-nitrohexane + O2 + H2O
hexanal + nitrite + H2O2
-
-
-
-
?
1-nitrohexane + O2 + H2O
hexanal + nitrite + H2O2
-
-
-
?
1-nitropropane + H2O + O2
propionaldehyde + nitrite + H2O2
-
-
-
-
?
1-nitropropane + H2O + O2
propionaldehyde + nitrite + H2O2
-
-
-
?
1-nitropropane + H2O + O2
propionaldehyde + nitrite + H2O2
-
-
-
-
?
1-nitropropane + H2O + O2
propionaldehyde + nitrite + H2O2
-
-
-
-
?
1-nitropropane + H2O + O2
propionaldehyde + nitrite + H2O2
-
-
-
-
?
1-nitropropane + H2O + O2
propionaldehyde + nitrite + H2O2
-
-
-
-
?
2-nitropropane + H2O + O2
acetone + nitrite + H2O2
-
-
-
-
?
2-nitropropane + H2O + O2
acetone + nitrite + H2O2
-
-
-
-
?
2-nitropropane + H2O + O2
acetone + nitrite + H2O2
-
-
-
-
?
nitroethane + H2O
ethanal + nitrite + H2O2
solvent isotope and viscositiy effects: the kcat proton inventory is consistent with a single exchangeable proton in flight, while the kcat/KM is consistent with either a single proton in flight in the transition state or a medium effect. Increasing the solvent viscosity does not affect the kcat or kcat/KM value significantly, establishing that nitroethane binding is at equilibrium and that product release does not limit kcat
-
-
?
nitroethane + H2O
ethanal + nitrite + H2O2
solvent isotope and viscositiy effects: the kcat proton inventory is consistent with a single exchangeable proton in flight, while the kcat/KM is consistent with either a single proton in flight in the transition state or a medium effect. Increasing the solvent viscosity does not affect the kcat or kcat/KM value significantly, establishing that nitroethane binding is at equilibrium and that product release does not limit kcat
-
-
?
nitroethane + H2O
ethanal + nitrite + H2O2
-
-
-
-
?
nitroethane + H2O
ethanal + nitrite + H2O2
-
-
-
?
nitroethane + H2O + O2
acetaldehyde + nitrite + H2O2
-
-
-
-
?
nitroethane + H2O + O2
acetaldehyde + nitrite + H2O2
-
-
-
-
?
nitroethane + O2
acetaldehyde + HNO2
-
-
-
-
?
nitroethane + O2
acetaldehyde + HNO2
-
production of H2O2
-
-
?
nitroethane + O2
acetaldehyde + HNO2
-
at pH 7, bi-ter ping-pong mechanism with oxygen reacting with the free reduced enzyme after release of the aldehyde product
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
-
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
nitroethane is the only substrate, of diverse primary and secondary alkanes, for which deprotonation is fully rate limiting for the reductive half reaction
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
O2 is delivered from air-saturated buffer in the assay reaction
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
the neutral substrate form is preferred, 5fold lower activity with the substrate anion, the D402 mutant enzymes in contrast prefer the anionic substrate form
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2 + H+
-
-
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2 + H+
-
-
-
ir
additional information
?
-
-
the physiological role of the enzyme is the oxidation of nitroaliphatic species
-
-
?
additional information
?
-
-
analysis of reaction intermediates formed by mass spectrometry and gel filtration
-
-
?
additional information
?
-
-
enzyme catalyzes the oxidation of nitroalkanes to the respective aldehydes or ketones with consumption of molecular oxygen and releasing nitrite and hydrogen peroxide
-
-
?
additional information
?
-
-
enzyme catalyzes the oxidation of primary and secondary nitroalkanes to the respective aldehydes or ketones, releasing nitrite
-
-
?
additional information
?
-
-
enzyme does not require anionic nitroalkanes for activity, enzyme catalyzes the oxidation of a number of primary and secondary nitroalkanes to the respective aldehydes or ketones with preference for primary nitroalkanes, monotonic increase with each additional methylene group from nitroethane to 1-nitrobutane increasing kcat/Km value by 20fold, no further increase with 1-nitropentane and 1-nitrohexane
-
-
?
additional information
?
-
-
enzyme shows high substrate specificity
-
-
?
additional information
?
-
-
the enzyme does not oxidize acyl-CoA substrates and prefers primary nitroalkanes containing four or more carbon atoms
-
-
-
additional information
?
-
-
slight activity, less than 5% of the activity towards nitroethane with: nitromethane, nitroacetic acid, 1-chloro-1-nitropropane, methylene blue also can function as hydrogen acceptor with low reaction rate
-
-
?
additional information
?
-
involved in the conversion of toxic nitroalkanes to less harmful compounds
-
-
?
additional information
?
-
-
involved in the conversion of toxic nitroalkanes to less harmful compounds
-
-
?
additional information
?
-
enzyme prefers the neutral forms of substrates and only reacts with anionic 2-nitropropane at a low rate
-
-
?
additional information
?
-
-
enzyme prefers the neutral forms of substrates and only reacts with anionic 2-nitropropane at a low rate
-
-
?
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Acute Coronary Syndrome
Long-term treatment with NAO in acute coronary syndromes: rationale and clinical data.
Adenoma
Fine needle aspiration diagnosis of hyperplastic and neoplastic follicular nodules of the thyroid. A morphometric study.
Alzheimer Disease
Tong Luo Jiu Nao, a Chinese Medicine Formula, Reduces Inflammatory Stress in a Mouse Model of Alzheimer's Disease.
Asthma
Irreversible airway obstruction assessed by high-resolution computed tomography (HRCT), exhaled nitric oxide (FENO), and biological markers in induced sputum in patients with asthma.
Asthma
[Determination and comparison of pulmonary function with anthropometric indexes in asthmatic and non-asthmatic obese teenagers]
Atrial Fibrillation
High CHA2DS2-VASc score without atrial fibrillation: 'NAO yes, NAO no'.
Brain Ischemia
Effect of Pei Yuan Tong Nao capsules on neuronal function and metabolism in cerebral ischemic rats.
Brain Ischemia
[Effect of nao shuan tong on the activity of SOD in cerebral tissues and NO in serums in the cerebral ischemia rats].
Brain Ischemia
[Influence of yi nao capsule on epinephrine and norepinephrine during rat ischemia].
Brain Ischemia
[The effect of yang xue qing nao granule on chronic cerebral ischemia]
Carcinoma
Fine needle aspiration diagnosis of hyperplastic and neoplastic follicular nodules of the thyroid. A morphometric study.
Cerebral Hemorrhage
Induction of NADPH-diaphorase activity in the forebrain in a model of intracerebral hemorrhage and its inhibition by the traditional Chinese medicine complex Nao Yi An.
Cerebral Hemorrhage
[Effects of plasma catecholamines contents on acute cerebral hemorrhage treated with nao yi-an granule]
Cerebral Palsy
A motor learning therapeutic intervention for a child with cerebral palsy through a social assistive robot.
Cerebrovascular Disorders
The development of nao li shen and its clinical application.
Cerebrovascular Disorders
The pharmacokinetic screening of multiple components of the Nao Mai Tong formula in rat plasma by liquid chromatography tandem mass spectrometry combined with pattern recognition method and its application to comparative pharmacokinetics.
Chickenpox
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Cleft Lip
Computational Analysis of the Mature Unilateral Cleft Lip Nasal Deformity on Nasal Patency.
Communicable Diseases
Climate variability and outbreaks of infectious diseases in Europe.
Communicable Diseases
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Congenital Abnormalities
Computational Analysis of the Mature Unilateral Cleft Lip Nasal Deformity on Nasal Patency.
Contracture
Submaximal sodium-lack contractures in rapidly perfused frog ventricular strips.
COVID-19
Covid-19: Poor links between NHS and social care weakened England's response, says NAO.
COVID-19
Covid-19: Test and trace system must improve its below par performance, NAO concludes.
Craniocerebral Trauma
The development of nao li shen and its clinical application.
Cysts
Dinoflagellate cysts and hydrographical change in Gullmar Fjord, west coast of Sweden.
Cysts
Hundred years of environmental change and phytoplankton ecophysiological variability archived in coastal sediments.
Dementia
Social robots in advanced dementia.
Dementia
Tong Luo Jiu Nao ameliorates A?1-40-induced cognitive impairment on adaptive behavior learning by modulating ERK/CaMKII/CREB signaling in the hippocampus.
Dementia, Multi-Infarct
Jian Nao Ning for treatment of memory impairment in patients with mild or moderate multi-infarct dementia.
Dementia, Vascular
Effect of Tong Luo Jiu Nao on A?-degrading enzymes in AD rat brains.
Dementia, Vascular
Effects of a traditional Chinese medicine, Qing Nao Yi Zhi Fang, on glutamate excitotoxicity in rat fetal cerebral neuronal cells in primary culture.
Dementia, Vascular
The diverse effects of a Chinese medicine, Qing Nao Yi Zhi Fang, on the proliferation of human arterial smooth muscle cells and endothelial cells.
Dementia, Vascular
Tong Luo Jiu Nao injection, a traditional Chinese medicinal preparation, inhibits MIP-1? expression in brain microvascular endothelial cells injured by oxygen-glucose deprivation.
Dysentery, Bacillary
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Encephalitis, Tick-Borne
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Encephalitis, Viral
Evaluation of the adjunctive effect of Xing Nao Jing Injection for viral encephalitis: A systematic review and meta-analysis of randomized controlled trials.
Endotoxemia
Effect of natural antioxidants and apocynin on LPS-induced endotoxemia in rabbit.
Endotoxemia
Effects of apocynin and natural antioxidant from spinach on inducible nitric oxide synthase and cyclooxygenase-2 induction in lipopolysaccharide-induced hepatic injury in rat.
Endotoxemia
The prophylactic effects of natural water-soluble antioxidant from spinach and apocynin in a rabbit model of lipopolysaccharide-induced endotoxemia.
Erysipelas
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Hajdu-Cheney Syndrome
A novel matrix metalloproteinase 2 (MMP2) terminal hemopexin domain mutation in a family with multicentric osteolysis with nodulosis and arthritis with cardiac defects.
Hemorrhagic Fever with Renal Syndrome
Time Series Analysis Performed on Nephropathia Epidemica in Humans of Northern Sweden in Relation to Bank Vole Population Dynamic and the NAO Index.
Hemorrhagic Stroke
[Effects of nao yi-an granule on hemorheological indexes and RCD (erythrocyte deformability) in patients with hemorrhagic stroke]
Hepatitis A
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Infections
Host-parasite interactions and global climate oscillations.
Infections
Patient safety and healthcare-associated infection.
Infectious Mononucleosis
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Ischemic Stroke
Tong Luo Jiu Nao injection, a traditional Chinese medicinal preparation, inhibits MIP-1? expression in brain microvascular endothelial cells injured by oxygen-glucose deprivation.
Joint Diseases
A novel matrix metalloproteinase 2 (MMP2) terminal hemopexin domain mutation in a family with multicentric osteolysis with nodulosis and arthritis with cardiac defects.
Joint Diseases
Radiological findings in NAO syndrome.
Leptospirosis
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Lyme Disease
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Measles
A link between the North Atlantic Oscillation and measles dynamics during the vaccination period in England and Wales.
Mumps
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Nasal Obstruction
Computational Analysis of the Mature Unilateral Cleft Lip Nasal Deformity on Nasal Patency.
Nasal Obstruction
Computed nasal resistance compared with patient-reported symptoms in surgically treated nasal airway passages: A preliminary report.
Nasal Obstruction
Correlation between Subjective Nasal Patency and Intranasal Airflow Distribution.
Nasal Obstruction
Diagnostic and Therapeutic Management of Nasal Airway Obstruction: Advances in Diagnosis and Treatment.
Nasal Obstruction
Endoscopic septoplasty: revisitation of the technique, indications, and outcomes.
Nasal Obstruction
Measuring Nasal Obstruction.
Nasal Obstruction
Nasal airway obstruction: Prevalence and anatomic contributors.
Nasal Obstruction
The impact of nasal adhesions on airflow and mucosal cooling - A computational fluid dynamics analysis.
Nasal Obstruction
The Impact of Nasal Obstruction and Functional Septorhinoplasty on Sleep Quality.
Neoplasms
Cancer incidence in the Nenetskij Avtonomnyj Okrug, Arctic Russia.
Neoplasms
Enhanced Cytotoxic Activity of Mitochondrial Mechanical Effectors in Human Lung Carcinoma H520 Cells: Pharmaceutical Implications for Cancer Therapy.
Occupational Diseases
Features of Occupational Health Risks in the Russian Arctic (on the Example of Nenets Autonomous Okrug and Chukotka Autonomous Okrug).
Osteolysis
Radiological findings in NAO syndrome.
Overweight
PROCEED: Prospective Obesity Cohort of Economic Evaluation and Determinants: baseline health and healthcare utilization of the US sample.
Papilloma
Topical and oral administration of the natural water-soluble antioxidant from spinach reduces the multiplicity of papillomas in the Tg.AC mouse model.
Plague
The delayed effect of cooling reinforced the NAO-plague connection in pre-industrial Europe.
Prostatic Neoplasms
Composition, efficacy, and safety of spinach extracts.
Renal Insufficiency
[Oliguric and non-oliguric renal failure in high risk patient in intensive care units (author's transl)]
Rhinitis
Correlations between computational fluid dynamics and clinical evaluation of nasal airway obstruction due to septal deviation: An observational study.
Salmonella Infections
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Scrub Typhus
[Study on the characteristics of Tsutsugamushi disease in the epidemic areas of south islands in China]
Seizures
Efficacy of ear-point stimulation on experimentally induced seizure.
Sepsis
The prophylactic effects of natural water-soluble antioxidant from spinach and apocynin in a rabbit model of lipopolysaccharide-induced endotoxemia.
Sinusitis
Correlations between computational fluid dynamics and clinical evaluation of nasal airway obstruction due to septal deviation: An observational study.
Spondylosis
The development of nao li shen and its clinical application.
Starvation
Unique natural antioxidants (NAOs) and derived purified components inhibit cell cycle progression by downregulation of ppRb and E2F in human PC3 prostate cancer cells.
Stroke
Effect of Tong Luo Jiu Nao on A?-degrading enzymes in AD rat brains.
Stroke
Effects of huo nao fang in 60 cases of ischemic apoplexy.
Stroke
Quicker response would improve stroke outcomes, NAO says.
Stroke
[Achievements and enlightenment of modern acupuncture therapy for stroke based on the neuroanatomy].
Surgical Wound Infection
Communicable disease and infection control: the surveillance contribution.
Thymoma
Cell quality control mechanisms maintain stemness and differentiation potential of P19 embryonic carcinoma cells.
Toxoplasmosis
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Tularemia
North Atlantic weather oscillation and human infectious diseases in the Czech Republic, 1951-2003.
Vascular Diseases
Effect of Pei Yuan Tong Nao capsules on neuronal function and metabolism in cerebral ischemic rats.
Vitamin E Deficiency
Vitamin E deficiency impairs the modifications of mitochondrial membrane potential and mass in rat splenocytes stimulated to proliferate.
Warts
Evaluation of mitochondrial content and activity with nonyl-acridine orange and rhodamine 123: flow cytometric analysis and comparison with quantitative morphometry. Comparative analysis by flow cytometry and quantitative morphometry of mitochondrial content and activity.
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0.03 - 0.18
1-nitrobutane
5.8 - 35.7
1-Nitropropane
83.5
2-Nitropropane
pH 8.0, 28°C
13.1
phenylacetic acid
-
-
additional information
additional information
-
0.03
1-nitrobutane
-
recombinant wild-type enzyme, pH 8.0, 30°C
0.18
1-nitrobutane
-
recombinant mutant D403E, pH 8.0, 30°C
0.04
1-nitrohexane
wild-type, pH 8.0, 30°C
0.2
1-nitrohexane
mutant S276A, pH 8.0, 30°C
0.03
1-nitrooctane
wild-type, pH 8.0, 30°C
0.3
1-nitrooctane
mutant S276A, pH 8.0, 30°C
5.8
1-Nitropropane
-
wild type enzyme, at 30°C, pH not specified in the publication
9.6
1-Nitropropane
-
mutant enzyme H183S, at 30°C, pH not specified in the publication
9.8
1-Nitropropane
-
mutant enzyme H183C, at 30°C, pH not specified in the publication
35.7
1-Nitropropane
pH 8.0, 28°C
0.042
nitroethane
-
pH 8.0, 30°C, mutant enzyme R409K
1.9
nitroethane
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2
nitroethane
-
mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2
nitroethane
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2.1
nitroethane
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2.1
nitroethane
mutant enzyme C397S, at pH 8.0 and 30°C
2.1
nitroethane
mutant enzyme S171A, at pH 8.0 and 30°C
2.3
nitroethane
-
recombinant wild-type enzyme, pH 8.0, 30°C
2.3
nitroethane
wild-type, pH 8.0, 30°C
2.3
nitroethane
wild type enzyme, at pH 8.0 and 30°C
2.3
nitroethane
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
3.3
nitroethane
mutant S276A, pH 8.0, 30°C
3.3
nitroethane
mutant enzyme S276A, at pH 8.0 and 30°C
4.8
nitroethane
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
4.8
nitroethane
mutant enzyme Y398F, at pH 8.0 and 30°C
5.4
nitroethane
-
wild type enzyme, at 30°C, pH not specified in the publication
8.1
nitroethane
-
mutant enzyme H183S, at 30°C, pH not specified in the publication
8.4
nitroethane
-
mutant enzyme H183C, at 30°C, pH not specified in the publication
10
nitroethane
mutant enzyme D399N, in 50 mM HEPES, pH 8.0, 30°C
13
nitroethane
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
14.6
nitroethane
-
recombinant mutant D403E, pH 8.0, 30°C
14.6
nitroethane
mutant enzyme D402E, at pH 8.0 and 30°C
24
nitroethane
mutant enzyme S273A, in 50 mM HEPES, pH 8.0, 30°C
25
nitroethane
mutant enzyme R406K, in 50 mM HEPES, pH 8.0, 30°C
26.3
nitroethane
-
pH 8.0, 30°C, mutant enzyme R409K
26.3
nitroethane
mutant enzyme R409K, at pH 8.0 and 30°C
26.8
nitroethane
pH 8.0, 28°C
0.011
O2
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.019
O2
-
pH 8.0, 30°C, mutant enzyme D402E
0.028
O2
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.029
O2
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.042
O2
-
pH 8.0, 30°C, mutant enzyme R409K
0.044
O2
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.058
O2
-
mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.082
O2
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.39
O2
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
additional information
additional information
-
kinetic competency of the cationic imine enzyme intermediate
-
additional information
additional information
-
kinetics and thermodynamics of the deprotonation step with substrate nitroethane, effects of tunneling
-
additional information
additional information
-
steady-state and rapid reaction kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
thermodynamics, kinetic mechanism with nitroethane and 1-nitrobutane, isotopic effects, monotonic increase with each additional methylene group from nitroethane to 1-nitrobutane increasing kcat/Km value by 20fold, no further increase with 1-nitropentane and 1-nitrohexane
-
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0.0006 - 0.024
1-Nitropropane
additional information
additional information
-
-
-
0.3
1-nitrohexane
mutant S276A, pH 8.0, 30°C
2
1-nitrohexane
wild-type, pH 8.0, 30°C
0.2
1-nitrooctane
mutant S276A, pH 8.0, 30°C
4.4
1-nitrooctane
wild-type, pH 8.0, 30°C
0.0006
1-Nitropropane
-
mutant enzyme H183C, at 30°C, pH not specified in the publication
0.00098
1-Nitropropane
-
mutant enzyme H183S, at 30°C, pH not specified in the publication
0.024
1-Nitropropane
-
wild type enzyme, at 30°C, pH not specified in the publication
0.00061
nitroethane
-
mutant enzyme H183C, at 30°C, pH not specified in the publication
0.0011
nitroethane
-
mutant enzyme H183S, at 30°C, pH not specified in the publication
0.031
nitroethane
-
wild type enzyme, at 30°C, pH not specified in the publication
0.037
nitroethane
mutant enzyme D399N, in 50 mM HEPES, pH 8.0, 30°C
1
nitroethane
mutant S276A, pH 8.0, 30°C
1
nitroethane
mutant enzyme S276A, at pH 8.0 and 30°C
2.4
nitroethane
cosubstrate D2O, 30°C, pH 8.5
2.6
nitroethane
-
pH 8.0, 30°C, mutant enzyme R409K
2.6
nitroethane
mutant enzyme R409K, at pH 8.0 and 30°C
3.1
nitroethane
mutant enzyme D402E, at pH 8.0 and 30°C
5
nitroethane
mutant enzyme S273A, in 50 mM HEPES, pH 8.0, 30°C
5.4
nitroethane
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
5.4
nitroethane
mutant enzyme C397S, at pH 8.0 and 30°C
5.4
nitroethane
mutant enzyme S171A, at pH 8.0 and 30°C
6.2
nitroethane
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
7.2
nitroethane
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
7.3
nitroethane
-
mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
9
nitroethane
mutant enzyme R406K, in 50 mM HEPES, pH 8.0, 30°C
10.6
nitroethane
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
11
nitroethane
mutant enzyme Y398F, at pH 8.0 and 30°C
15
nitroethane
wild-type, pH 8.0, 30°C
15
nitroethane
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
15
nitroethane
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
15
nitroethane
wild type enzyme, at pH 8.0 and 30°C
2.6
O2
-
pH 8.0, 30°C, mutant enzyme R409K
15
O2
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
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0.000062 - 0.0042
1-Nitropropane
0.000073 - 6.3
nitroethane
0.000062
1-Nitropropane
-
mutant enzyme H183C, at 30°C, pH not specified in the publication
0.0001
1-Nitropropane
-
mutant enzyme H183S, at 30°C, pH not specified in the publication
0.0042
1-Nitropropane
-
wild type enzyme, at 30°C, pH not specified in the publication
0.000073
nitroethane
-
mutant enzyme H183C, at 30°C, pH not specified in the publication
0.00013
nitroethane
-
mutant enzyme H183S, at 30°C, pH not specified in the publication
0.004
nitroethane
mutant enzyme D399N, in 50 mM HEPES, pH 8.0, 30°C
0.0057
nitroethane
-
wild type enzyme, at 30°C, pH not specified in the publication
0.098
nitroethane
mutant enzyme R409K, at pH 8.0 and 30°C
0.21
nitroethane
mutant enzyme S273A, in 50 mM HEPES, pH 8.0, 30°C
0.21
nitroethane
mutant enzyme D402E, at pH 8.0 and 30°C
0.3
nitroethane
mutant enzyme S276A, at pH 8.0 and 30°C
0.37
nitroethane
mutant enzyme R406K, in 50 mM HEPES, pH 8.0, 30°C
0.6
nitroethane
cosubstrate D2O, 30°C, pH 8.5
0.74
nitroethane
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
2.2
nitroethane
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2.2
nitroethane
mutant enzyme Y398F, at pH 8.0 and 30°C
2.6
nitroethane
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2.6
nitroethane
mutant enzyme C397S, at pH 8.0 and 30°C
2.6
nitroethane
mutant enzyme S171A, at pH 8.0 and 30°C
3.2
nitroethane
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
3.6
nitroethane
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
6.3
nitroethane
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
6.3
nitroethane
wild type enzyme, at pH 8.0 and 30°C
38
O2
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
140
O2
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
190
O2
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
290
O2
-
mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
310
O2
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
390
O2
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
580
O2
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
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crystallization data of mutant D402N in complex with 1-nitrohexane or 1-nitrooctane show the presence of substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD. The structure of wild-type enzyme trapped with cyanide during oxidation of 1-nitrohexane shows the presence of the modified flavin. A continuous hydrogen bond network connects the nitrogen of the CN-hexyl-FAD through the FAD 2'-hydroxyl to a chain of water molecules extending to the protein surface. Data for mutant S276A in complex with nitrohexane
hanging drop vapour diffusion method
-
hexagonal rod-shaped crystals of R409K and D402E NAO were obtained using hanging drop vapor-diffusion methods
-
purified recombinant wild-type enzyme, crystallization of the native enzyme in 2 different crystal forms and of the selenomethionine-labeled enzyme in a third one, hanging drop vapour diffusion method, sodium cacodylate buffer, pH 7.5, containing spermidine hydrochloride, and PEG 4000 at varying concentrations for all 3 mixtures, crystal form 2 requires addition of 1,6-hexanediol at 8% w/v, crystal form 3 requires DTT at 10 mM, 4°C, 10-14 days, X-ray diffraction structure determinations and analysis at 3.2-2.0 A resolution or below, three-wavelength MAD data
-
vapor diffusion method, using 2.5 M magnesium sulfate, 0.1 M 2-(N-morpholino) ethanesulfonic acid buffer, pH 6.0, and 18% (v/v) glycerol
mutant enzyme H183S in complex with nitroethane and FMN, hanging drop vapor diffusion method, using 0.2 M ammonium fluoride, 20% (w/v) polyethylene glycol 3350
-
native and a selenomethionine-substituted enzyme, to 1.9 A resolution. Primitive orthorhombic space group P21, with unit-cell parameters a = 70.06, b = 55.43, c = 87.74 A, beta = 96.56° for native NAO and a = 69.89, b = 54.83, c = 88.20 A, beta = 95.79° for selenomethionine-substituted enzyme
-
wild-type and mutant H179D. Enzyme consists of two domains, a TIM barrel domain bound to FMN and C-terminal domain with a alpha-alpha-alpha-beta-alpha-beta-alpha fold. It shows the typical function as nitroalkane oxidase but its structure is similar to that of 2-nitropropane dioxygenase
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D402A
-
site-directed mutation of the active site base, 20fold reduced catalytic efficiency with neutral nitroethane as substrate compared to the wild-type enzyme, while the wild-type enzyme prefers the neutral substrate the mutant prefers the anion substrate form, altered pH-dependence with both substrate forms compared to the wild-type enzyme
S171T
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation
S171V
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation
D399N
the mutation decreases the kcat/KM value for nitroethane over 2 orders of magnitude
R406K
the mutation decreases the kcat/KM value for nitroethane about 64fold
S373A
the mutation decreases the kcat/KM value for nitroethane about 3fold
H183C
-
the mutant shows reduced activity compared to the wild type enzyme
H183S
-
the mutant shows reduced activity compared to the wild type enzyme
H179D
residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity
H179K
residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity
H179V
residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity
C397S
the mutant shows reduced activity compared to the wild type enzyme
C397S
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutant enzyme is less stable than the wild type enzyme
D402E
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, mutation has no effect on the rate of reaction of the reduced enzyme with oxygen, reaction mechanism analysis
D402E
-
mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme, determined at 2.4 A resolution, shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402. The interaction of this residue with Ser276 is perturbed
D402E
-
the mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402 (compared to mutant enzyme R409K), and the interaction of this residue with Ser276 is perturbed
D402E
the mutant shows severely reduced activity compared to the wild type enzyme
D402N
-
site-directed mutation of the active site base, 140fold reduced catalytic efficiency with neutral nitroethane as substrate compared to the wild-type enzyme, while the wild-type enzyme prefers the neutral substrate the mutant prefers the anion substrate form, altered pH-dependence with both substrate forms compared to the wild-type enzyme
D402N
no detectable activity with neutral substrates. Crystallization data in complex with 1-nitrohexane or 1-nitrooctane show the presence of substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD
D402N
the mutant shows reduced activity compared to the wild type enzyme
R409K
-
the mutation results in a decrease in the rate constant for proton abstraction of 100fold. Analysis of the three-dimensional structure of the R409K enzyme shows that the critical structural change is an increase in the distance between the carboxylate of Asp402 and the positively charged nitrogen in the side chain of the residue at position 409
R409K
-
the mutation results in a decrease in the rate constant for proton abstraction of 100fold. Analysis of the three-dimensional structure of the R409K enzyme, determined by X-ray crystallography to a resolution of 2.65 A, shows that the critical structural change is an increase in the distance between the carboxylate of Asp402 and the positively charged nitrogen in the side chain of the residue at position 409
R409K
the mutant shows severely reduced activity compared to the wild type enzyme
S171A
the mutant shows reduced activity compared to the wild type enzyme
S171A
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold
S276A
more than 20fold decrease in catalytic efficiency
S276A
the mutant shows severely reduced activity compared to the wild type enzyme
Y398F
the mutant shows reduced activity compared to the wild type enzyme
Y398F
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutant enzyme is less stable than the wild type enzyme
additional information
naoA disruption accelerates growth of the naoA-disruption mutant, which can restore its phenotype and morphology as a wild-type strain by complementation of a single copy number of naoA inserted into the chromosome. The introduction of an extra copy of naoA into the wild-type strain results in delayed growth
additional information
-
naoA disruption accelerates growth of the naoA-disruption mutant, which can restore its phenotype and morphology as a wild-type strain by complementation of a single copy number of naoA inserted into the chromosome. The introduction of an extra copy of naoA into the wild-type strain results in delayed growth
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Little, H.N.
Oxidation of nitroethane by extracts from Neurospora
J. Biol. Chem.
193
347-358
1951
Neurospora crassa
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Kinetic mechanism and substrate specificity of nitroalkane oxidase
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Fusarium oxysporum
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Mechanism of nitroalkane oxidase: 2. pH and kinetic isotope effects
Biochemistry
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2000
Fusarium oxysporum
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Iso-mechanism of nitroalkane oxidase: 1. Inhibition studies and activation by imidazole
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2000
Fusarium oxysporum
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Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum
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Fusarium oxysporum
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Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily
Proc. Natl. Acad. Sci. USA
99
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2002
Fusarium oxysporum
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Crystallization and preliminary analysis of active nitroalkane oxidase in three crystal forms
Acta Crystallogr. Sect. D
60
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2004
Fusarium oxysporum
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Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase
Arch. Biochem. Biophys.
433
157-165
2005
Fusarium oxysporum
brenda
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Reductive half-reaction of nitroalkane oxidase: effect of mutation of the active site apartate to glutamate
Biochemistry
42
5850-5856
2003
Fusarium oxysporum
brenda
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Inactivation of nitroalkane oxidase upon mutation of the active site base and rescue with a deprotonated substrate
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125
8738-8739
2003
Fusarium oxysporum
brenda
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Comparison of enzymatic and nonenzymatic nitroethane anion formation: thermodynamics and contribution of tunneling
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126
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2004
Fusarium oxysporum
brenda
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Establishing the kinetic competency of the cationic imine intermediate in nitroalkane oxidase
J. Am. Chem. Soc.
127
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2005
Fusarium oxysporum
brenda
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Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover
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45
1138-1150
2006
Fusarium oxysporum
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Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase
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46
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2007
Fusarium oxysporum
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Crystal structures of intermediates in the nitroalkane oxidase reaction
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48
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Fusarium oxysporum (Q8X1D8)
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Identification of a nitroalkane oxidase gene: naoA related to the growth of Streptomyces ansochromogenes
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57
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Streptomyces ansochromogenes (Q9FDD4), Streptomyces ansochromogenes
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Identification of a hypothetical protein from Podospora anserina as a nitroalkane oxidase
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49
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Podospora anserina (B2AM55), Podospora anserina
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Characterization of active site residues of nitroalkane oxidase
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Fusarium oxysporum
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69
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2013
Pseudomonas aeruginosa
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Crystal structure and site-directed mutagenesis of a nitroalkane oxidase from Streptomyces ansochromogenes
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405
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2011
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Nitroalkane oxidase Structure and mechanism
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Crystal structure of hypothetical protein PA4202 from Pseudomonas aeruginosa PAO1 in complex with nitroethane as a nitroalkane substrate
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503
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Pseudomonas aeruginosa
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Genetically engineered thermotolerant facultative anaerobes for high-efficient degradation of multiple hazardous nitroalkanes
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