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Results for “Hydroxylamine”

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At least 19 recordsLinked to original sources

PubMedDate not supplied

N-oxygenation of primary amines and hydroxylamines and retroreduction of hydroxylamines by adult human liver microsomes and adult human flavin-containing monooxygenase 3.

Adult human liver microsomes catalyze the NADPH-dependent N-oxygenation of 10-N-(n-octylamino)-2-(trifluoromethyl)phenothiazine to the corresponding oximes through the intermediacy of the hydroxylamine. In the presence of adult human liver microsomes, the primary amine is stereoselectively converted to the cis-oxime, but addition of the alternative competitive substrate hydroxylamine hydrochloride apparently decreases the amount of aliphatic hydroxylamine retroreduction because an increase in oxime formation was observed. In the presence of hydroxylamine hydrochloride, however, the oxime product recovered was formed with very low stereoselectivity. Studies on the biochemical mechanism of oxime formation suggested that cis-oxime formation in the presence of adult human liver microsomes was largely dependent on the human flavin-containing monooxygenase (form 3). This conclusion is based on the effects of incubation conditions on product formation when compared to results observed in the presence of cDNA-expressed human FMO3. The retroreduction of the intermediate hydroxylamine was dependent on NADPH but was not catalyzed by human flavin-containing monooxygenase (form 3) or any one of seven prominent cytochromes P-450 that have been well-characterized in the human liver microsomes examined. The results suggest that aliphatic primary amines are efficiently sequentially N-oxygenated in the presence of human liver microsomes to hydroxylamines and then to oximes mainly by the human flavin-containing monooxygenase. Retroreduction of the intermediate hydroxylamine is apparently facilitated by a novel but as yet poorly characterized enzyme system that does not employ any of the currently known well-characterized cytochrome P-450 enzymes present in adult human liver microsomes.

Adolescent↗

PubMed1997

Hydroxylamine metabolism in Pseudomonas PB16: involvement of a novel hydroxylamine oxidoreductase.

Pseudomonas strain PB16, a Gram-negative heterotrophic nitrifying bacterium closely related to Pseudomonas azalaica on the basis of 16 S rDNA analysis, was able to use hydroxylamine as an additional energy source during growth in acetate limited chemostat cultures giving an increased biomass yield. In aerobically growing cells of Pseudomonas PB16 only 50% of supplemented hydroxylamine could be recovered as nitrite. In addition to nitrite, N2O could be detected in the chemostat off-gas, indicating combined heterotrophic nitrification and aerobic denitrification. The maximum specific hydroxylamine oxidizing activity observed was 450 nmol per min per mg dry weight, with a Ks of approximately 40 microM. Upon addition of hydroxylamine to the medium, Pseudomonas PB16 induced a soluble 132 KDa dimeric hydroxylamine oxidoreductase. The enzyme had a pH optimum of 9, and did not contain spectroscopic features typical for cytochromes, which is in contrast to hydroxylamine oxidoreductases found in autotrophic bacteria.

Acetates↗

PubMed2000

Reduction of amphetamine hydroxylamine and other aliphatic hydroxylamines by benzamidoxime reductase and human liver microsomes.

For the reduction of N-hydroxylated derivatives of strongly basic functional groups, such as amidines, guanidines, and aminohydrazones, an oxygen-insensitive liver microsomal system, the benzamidoxime reductase, has been described. To reconstitute the complete activity of the benzamidoxime reductase, the system required cytochrome b(5), NADH-cytochrome b(5)-reductase, and the benzamidoxime reductase, a cytochrome P450 enzyme, which has been purified to homogeneity from pig liver. It was not known if this enzyme system was also capable of reducing aliphatic hydroxylamines. The N-hydroxylation of aliphatic amines is a well-known metabolic process. It was of interest to study the possibility of benzamidoxime reductase reducing N-hydroxylated metabolites of aliphatic amines back to the parent compound. Overall, N-hydroxylation and reduction would constitute a futile metabolic cycle. As examples of medicinally relevant compounds, the hydroxylamines of methamphetamine, amphetamine, and N-methylamine as model compounds were investigated. Formation of methamphetamine and amphetamine was analyzed by newly developed HPLC methods. All three hydroxylamines were easily reduced by benzamidoxime reductase to their parent amines with reduction rates of 220.6 nmol min(-1) (mg of protein)(-1) for methamphetamine, 5.25 nmol min(-1) (mg of protein)(-1) for amphetamine, and 153 nmol min(-1) (mg of protein)(-1) for N-methylhydroxylamine. Administration of synthetic hydroxylamines of amphetamine and methamphetamine to primary rat neuronal cultures produced frank cell toxicity. Compared with amphetamine or the oxime of amphetamine, the hydroxylamines were significantly more toxic to primary neuronal cells. The benzamidoxime reductase is therefore involved in the detoxication of these reactive hydroxylamines.

Amphetamines↗

PubMed1996

Hydroxylamine oxidation in heterotrophic nitrate-reducing soil bacteria and purification of a hydroxylamine-cytochrome c oxidoreductase from a Pseudomonas species.

Hydroxylamine oxidation was measured in four recently isolated heterotrophic nitrate-reducing bacteria belonging to the genera Pseudomonas, Moraxella, Arthrobacter and Aeromonas. A hydroxylamine-cytochrome c oxidoreductase activity was detected in periplasmic fractions of the Pseudomonas and Aeromonas spp. and in total soluble fractions of the Arthrobacter sp. A monomeric 19-kDa non-haem iron hydroxylamine-cytochrome c oxidoreductase was purified from the Pseudomonas species and shown to be similar to hydroxylamine-cytochrome c oxidoreductase of Paracoccus denitrificans.

Aeromonas↗

PubMed2001

Antioxidative activity of hydroxylamines. ESR spectra of radicals derived from hydroxylamines.

The antioxidative activity of hydroxylamines was evaluated for the oxidation of tetralin at 61 degrees C and linoleic acid micelles in an aqueous dispersion at 37 degrees C, induced by an azo initiator. The antioxidative efficacy of the hydroxylamines for the oxidation of tetralin was smaller than that of alpha-tocopherol. However, the hydroxylamines showed more potent antioxidative activity than that of the alpha-tocopherol against the oxidation of linoleic acid micelles. On the basis of the results of an ESR study and the oxidation product obtained, it is suggested that active position in hydroxylamines depend not only on hydroxyl hydrogen-atom, but also on the allylic hydrogen atom.

Antioxidants↗

PubMed2004

Hydroxylamine assimilation by Rhodobacter capsulatus E1F1. requirement of the hcp gene (hybrid cluster protein) located in the nitrate assimilation nas gene region for hydroxylamine reduction.

Rhodobacter capsulatus E1F1 grows phototrophically with nitrate as nitrogen source. Using primers designed for conserved motifs in bacterial assimilatory nitrate reductases, a 450-bp DNA was amplified by PCR and used for the screening of a genomic library. A cosmid carrying an insert with four SalI fragments of 2.8, 4.1, 4.5, and 5.8 kb was isolated, and DNA sequencing revealed that it contains a nitrate assimilation (nas) gene region, including the hcp gene coding for a hybrid cluster protein (HCP). Expression of hcp is probably regulated by a nitrite-sensitive repressor encoded by the adjacent nsrR gene. A His(6)-HCP was overproduced in Escherichia coli and purified. HCP contained about 6 iron and 4 labile sulfide atoms per molecule, in agreement with the presence of both [2Fe-2S] and [4Fe-2S-2O] clusters, and showed hydroxylamine reductase activity, forming ammonia in vitro with methyl viologen as reductant. The apparent K(m) values for NH(2)OH and methyl viologen were 1 mM and 7 microM, respectively, at the pH and temperature optima (9.3 and 40 degrees C). The activity was oxygen-sensitive and was inhibited by sulfide and iron reagents. R. capsulatus E1F1 grew phototrophically, but not heterotrophically, with 1 mM NH(2)OH as nitrogen source, and up to 10 mM NH(2)OH was taken up by anaerobic resting cells. Ammonium was transiently accumulated in the media, and its assimilation was prevented by L-methionine-D,L-sulfoximine, a glutamine synthetase inhibitor. In addition, hydroxylamine- or nitrite-grown cells showed the higher hydroxylamine reductase activities. However, R. capsulatus B10S, a strain lacking the whole hcp-nas region, did not grow with 1 mM NH(2)OH. Also, E. coli cells overproducing HCP tolerate hydroxyl-amine better during anaerobic growth. These results suggest that HCP is involved in assimilation of NH(2)OH, a toxic product that could be formed during nitrate assimilation, probably in the nitrite reduction step.

Amino Acid Sequence↗

PubMed2001

Interaction between dioxoruthenium(VI) porphyrins and hydroxylamines: coordination of N-substituted hydroxylamine to ruthenium and X-ray crystal structures of ruthenium complexes with a unidentate nitrosoarene ligand.

The interactions between dioxoruthenium(VI) porphyrins 1 with N-phenylhydroxylamine or unsubstituted hydroxylamine are described. Reaction of complexes 1 with excess PhNHOH leads to isolation of bis(nitrosobenzene)ruthenium(II) porphyrins 3 and mono(nitrosobenzene)ruthenium(II) porphyrins 4. Both the types of ruthenium complexes are characterized by 1H NMR, IR, and UV/Vis spectroscopy, and mass spectrometry. The X-ray structure determinations on [Ru(II)(TPP)(PhNO)2] (3a), [Ru(II)(2,6-Cl-TPP)(PhNO)2] (3e), and [Ru(II)(4-MeO-TPP)(PhNO)(PhNH2)] (4d) (TPP tetraarylporphyrin) disclose a unidentate nitrosoarene coordination in all these complexes, with Ru-N(PhNO) bond lengths of 2.003(3) (3a, average), 1.991(3) (3e, average), and 2.042(2) A (4d). In the case of 4d, the Ru-N(PhNH2) bond length is found to be 2.075(3) A. Mechanistic investigations reveal the formation of intermediates [Ru(II)(Por)(PhNO)(PhNHOH)] (5; Por=porphyrin), a ruthenium complex with N-substituted hydroxylamine ligand, in the "1 + PhNHOH" system. The Ru-NH(OH)Ph moiety in 5 undergoes no rapid exchange with free PhNHOH in solution at room temperature, as revealed by 1H NMR spectroscopy. Unlike the interaction between complexes 1 and PhNHOH, reaction of such complexes with NH2OH affords nitrosylruthenium(II) porphyrins [Ru(II)(Por)(NO)(OH)] (6).

Catalysis↗

PubMed1978

The mechanism of the mutagenic action of hydroxylamine XIII. Reversion of phage MS2 amber mutants in the presence of hydroxylamines.

The replication of the phage MS2 in the presence of either hydroxylamine (HA) or O-methylhydroxylamine (OMHA) (mutagenesis in vivo) results in an increase in the reversion frequency of two amber mutations in the maturation protein. When acting on the extracellular phage (mutagenesis in vitro) the mutagens do not affect the reversion frequency. The most probable mode of mutagenic action of the hydroxylamines on the vegetative MS2 phage involves the enzymic formation of modified precursors and their incorporation into RNA.

Coliphages↗

PubMed1975

Effects of hydroxylamine on the consequences of long-lasting administration of morphine in mice. II. Time course of the hydroxylamine effect on morphine tolerance.

Mice injected for 35 days with morphine sulfate in increasing doses did not show tolerance to the analgesic effects of morphine if injected intracranially with 0.3 M hydroxylamine. The excitatory action of morphine was unaffected. The interference with tolerance lasted for at least six weeks following the hydroxylamine injection. There were no apparent histological changes in the brains of treated mice as well as no differences in the composition of water-soluble brain proteins.

Animals↗

PubMed1978

The mechanism of the mutagenic action of hydroxylamine XII. Phenotypic suppression of amber mutants of phage T7 by hydroxylamine and O-methylhydroxylamine.

The reproduction of phage T7 in the presence of hydroxylamine (HA) (mutagenesis in vivo) results in the phenotypic suppression of some amber mutants. The presence of O-methylhydroxylamine (OMHA) results in a similar effect, indicating a similar mechanism for the action of the two compounds. Since the rate of reaction of mutagen with nucleoside residues under these conditions in negligibly low, one of the most plausible explanations of this effect is the enzymic formation of modified precursors and their incorporation into bacterial tRNAs or phage-induced RNA.

Coliphages↗

PubMed1963