Disease relevance of Nitrosomonas

• Incorporation of 13C from [13C]urea was low but significant, and the largest amounts of urea-derived C were found in common fatty acids (i.e., 16:0, 16:1omega7c, and 18:1omega7) that would be consistent with growth of typical NH4(+)-oxidizing (Nitrosomonas) and NO2(-)-oxidizing (Nitrobacter) bacteria [1].
• We have found that DPI inhibits both membrane-bound methane monooxygenase (pMMO) from Methylococcus capsulatus and ammonia monooxygenase (AMO) of Nitrosomonas europaea [2].
• The cytochrome reacted rapidly with pseudomonas aeruginosa nitrite reductase [EC 1.9.3.2], but slowly with bovine cytochrome oxidase [EC 1.9.3.1], yeast cytochrome c peroxidase [EC 1.11.1.5], or Nitrosomonas europaea hydroxylamine-cytochrome c reductase [EC 1.7.3.4] [3].
• With the aid of multidimensional scaling (MDS), a multivariate statistical method, we examined the toxicity data of five bioassays (the continuous Shk1, Polytox, activated sludge respiration inhibition, Nitrosomonas, and Tetrahymena assays) that could serve as test battery components for the assessment of wastewater toxicity to activated sludge [4].
• The gene organization of the cytochrome showed some resemblance to cytochrome c clusters of unknown function in the genome of Nitrosomonas europaea and Geobacter sulfurreducens PCA [5].

High impact information on Nitrosomonas

• The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea [6].
• From recent research it has become clear that at least two different possibilities for anaerobic ammonium oxidation exist in nature. 'Aerobic' ammonium oxidizers like Nitrosomonas eutropha were observed to reduce nitrite or nitrogen dioxide with hydroxylamine or ammonium as electron donor under anoxic conditions [7].
• A distinctive electrocatalytic response from the cytochrome c peroxidase of nitrosomonas europaea [8].
• A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states [9].
• 14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase [10].

Chemical compound and disease context of Nitrosomonas

• NH2OH, the first intermediate in the oxidation of NH4+ to nitrite by the nitrifying bacterium, Nitrosomonas europaea, was recovered as the oxime of cyclohexanone [11].
• Hydroxylamine oxidoreductase from Nitrosomonas europeae catalyzes the oxidative conversion of NH2OH to NO-2 [12].
• Mössbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting [12].
• Methane inhibited NH4+ utilization by Nitrosomonas europaea with a Ki of 2mM [13].
• In the presence of a suitable electron acceptor such as mammalian cytochrome c, hydroxylamine oxidoreductase (HAO) from the chemolithotrophic bacterium Nitrosomonas europaea catalyzes the oxidation of hydroxylamine or hydrazine to nitrite or dinitrogen, respectively [14].

Biological context of Nitrosomonas

• The migration of deuterium and hydrogen was observed in the aromatic hydroxylation of specifically deuterated, monosubstituted benzenes catalyzed by ammonia monooxygenase of Nitrosomonas europaea [15].
• Hydroxylamine oxidoreductase (HAO) from the autotrophic nitrifying bacterium Nitrosomonas europaea catalyzes the oxidation of NH2OH to NO2-. The enzyme contains eight hemes per subunit which participate in catalysis and electron transport [16].
• Although Nitrosomonas europaea lacks measurable alpha-ketoglutarate dehydrogenase activity, the recent completion of the genome sequence revealed the presence of the genes encoding the enzyme [17].
• Mutagenesis of hydroxylamine oxidoreductase in Nitrosomonas europaea by transformation and recombination [18].
• Oligonucleotide primers, based on the published amoA sequence from Nitrosomonas europaea, were used to amplify DNA from pure cultures of Nitrosomonas europaea, Nitrosomonas cryotolerans, and Nitrosococcus oceanus and from bacteria in seawater collected offshore near the Florida Keys [19].

Anatomical context of Nitrosomonas

• However, 14C-labeled forms of the membrane-bound, active-site-containing 27 kDa polypeptide of ammonia monooxygenase from Nitrosomonas europaea undergo an aggregation reaction when cells or membranes are heated in the presence of SDS-PAGE sample buffer [20].

Gene context of Nitrosomonas

• The dnaK gene of an ammonia-oxidizing bacterium, Nitrosomonas europaea, was cloned and sequenced [21].
• Isolation and characterization of cbbL and cbbS genes encoding form I ribulose-1,5-bisphosphate carboxylase/oxygenase large and small subunits in Nitrosomonas sp. strain ENI-11 [22].
• The cbbL and cbbS genes encoding form I ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) large and small subunits in the ammonia-oxidizing bacterium Nitrosomonas sp. strain ENI-11 were cloned and sequenced [22].
• The complete nucleotide sequences of the Nitrosomonas europaea grpE and dnaJ genes were determined [23].
• Expression of nitrite reductase in Nitrosomonas europaea involves NsrR, a novel nitrite-sensitive transcription repressor [24].

Analytical, diagnostic and therapeutic context of Nitrosomonas

• The phenotypes of three different Nitrosomonas europaea strains--wild-type, nitrite reductase (NirK)-deficient and nitric oxide reductase (NorB)-deficient strains--were characterized in chemostat cell cultures, and the effect of nitric oxide (NO) on metabolic activities was evaluated [25].
• Hydroxylamine oxidoreductase [EC 1.7.3.4] from Nitrosomonas europaea was crystallized by the microdialysis method using ammonium sulfate [26].
• However, in situ hybridization results revealed that the addition of NH2OH changed the form of growth pattern of the dominant Nitrosomonas spp. from dense clusters mode to single scattered cells mode [27].
• The effect of solids retention time (SRT) on ammonia-and nitrite-oxidizing bacteria was measured by Nitrosomonas oligotropha-like ammonia monooxygenase A and Nitrospira 16S rDNA competitive polymerase chain reaction assays in a complete-mix, bench-scale, activated-sludge system [28].
• As a result, it was possible to detect and quantify amoA expression in cultured Nitrosomonas europaea and even complex microbial communities such as nitrifying bacterial aggregates by competitive RT-PCR [29].

References