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PubMed1975

Pyridine-2, 6-dicarboxylic acid (dipicolinic acid) formation in Bacillus subtilis. II Non-enzymatic and enzymatic formations of dipicolinic acid from alpha, epsilon-diketopimelic acid and ammonia.

Non-enzymatic formation of dipicolinic acid (DPA) from diketopimelic acid and ammonia was clearly demonstrated using a new method for DPA analysis. The reaction rates of DPA formation were almost the same under aerobic and anaerobic conditions. Nearly equimolecular quantities of DPA and tetrahydrodipicolinic acid were detected in spontaneous reaction mixture. The spontaneous reaction seemed to be due to dismutation of dihydrodipicolinic acid, resulting in DPA and tetrahydrodipicolinic acid. The apparent optimum pH of the spontaneous reaction was 8.2 and the maximal rate of DPA formation was observed with a 1 : 4 molar ratio of diketopimelic acid to ammonia. The rate of the spontaneous reaction was stimulated by ferrous sulfate, FMN, and riboflavin. Dihydrodipicolinate reductase catalyzes the reduction of dihydrodipicolinate, prepared from pyruvate and aspartic beta-semialdehyde, with NADPH as reductant. The reductase was isolated from Bacillus subtilis, and found to stimulate DPA formation from diketopimelic acid and ammonia. The enzymatic DPA formation was absolutely dependent on oxygen, and optimum pH was 6.4. The catalytic action of the enzyme was similar to that of the oxidase. Possible mechanisms of DPA formation from diketopimelic acid and ammonia are proposed.

Aerobiosis↗
PubMed1972

A possible role of divalent manganese ions in the photoinduction of phenylalanine ammonia-lyase.

Divalent Mn ions cause an increase in the level of phenylalanine ammonia-lyase in gherkin hypocotyls. With the exception of Mg ions, which had a small effect, no other metal ion has so far been found which could replace the Mn ion in this respect. Invertase and peroxidase were not significantly affected by the Mn treatment. The increase in phenylalanine ammonialyase activity is explained by the removal, under the influence of Mn ions, of hydroxycinnamic acids, which cause repression of phenylalanine ammonia-lyase synthesis and/or inactivation of phenylalanine ammonia-lyase. Arguments are advanced for the hypothesis that photochemical transformations of Mn complexes are involved in the photoinduction of phenylalanine ammonia-lyase in dark-grown gherkin seedlings.

Journal Article↗
PubMed1982

Regulation by amino acids of photorespiratory ammonia and glycolate release from ankistrodesmus in the presence of methionine sulfoximine.

Methionine sulfoximine induced release of ammonia from illuminated cells of Ankistrodesmus braunii (Naegeli) Brunnth, in normal air, but less in air enriched to 3% CO(2). In normal air, methionine sulfoximine also induced glycolate release. Addition of either glutamate, glycine, or serine suppressed glycolate release, whereas glutamate and glycine at the same time stimulated ammonia release. The results indicate that inhibition of glutamine synthetase and thereby inhibition of photorespiratory nitrogen cycling restricts the sink capacity for glycolate in the photorespiratory carbon cycle. An external supply of glutamate, glycine, or serine seems to stimulate glyoxylate transamination and thus partly restores the sink capacity. Calculations of total glycolate formation rates in air from glycolate and ammonia release rates in the presence of methionine sulfoximine and glutamate revealed values of approximately 20 micromoles glycolate per milligram chlorophyll per hour on the average. Similar calculations led to an estimated rate of photorespiratory ammonia release in air, in the absence of methionine sulfoximine, of about 10 micromoles per milligram chlorophyll per hour on the average, a value comparable to the primary nitrogen assimilation rate of 8 micromoles per milligram chlorophyll per hour.

Journal Article↗
PubMed1985

Tyrosine and Phenylalanine Ammonia Lyase Activities during Shoot Initiation in Tobacco Callus Cultures.

Both phenylalanine ammonia lyase and tyrosine ammonia lyase were detected in tobacco (Nicotiana tabacum L. Wisconsin 38) callus. The enzymes were separated from each other by Sephadex G-200 column chromatography. Increased activity of tyrosine ammonia lyase was observed during culture of tobacco callus under shoot-forming conditions, while activity of phenylalanine ammonia lyase increased during culture under non-organ-forming conditions. Confirmation of these findings was obtained by examining the incorporation of [(14)C]tyrosine and [(14)C]phenylalanine into p-coumarate and trans-cinnamate, respectively.

Journal Article↗
PubMed2000

Molecular analysis of ammonia-oxidising bacteria in soil of successional grasslands of the Drentsche A (The Netherlands).

Changes in the community structure of chemolitho-autotrophic ammonia-oxidising bacteria of the beta-subgroup Proteobacteria were monitored during nutrient-impoverishment management of slightly acidic, peaty grassland soils, which decreased in pH with succession. Specific PCR, cloning and sequence analysis, denaturing gradient gel electrophoresis (DGGE) and probe hybridisation were used to analyse rDNA sequences directly recovered from successional soils. Four previously characterised ammonia oxidiser sequence clusters were recovered from each soil, three associated with the genus Nitrosospira and one with the genus Nitrosomonas. All samples were dominated by Nitrosospira-like sequences. Nitrosospira cluster 3 was the most commonly recovered ammonia oxidiser group in all fields, but a greater representation of Nitrosospira clusters 2 and 4 was observed in older fields. Most probable number (MPN) counts were conducted using neutral and slightly acid conditions. Neutral pH (7.5) MPNs suggested a decrease in ammonia oxidiser numbers in later successional fields, but this trend was not observed using slightly acid (pH 5.8) conditions. Analysis of terminal MPN dilutions revealed a distribution of sequence clusters similar to direct soil DNA extractions. However, an increased relative recovery of Nitrosospira cluster 2 was observed for acid pH MPNs compared to neutral pH MPNs from the most acidic soil tested, in agreement with current hypotheses on the relative acid tolerance of this group.

Journal Article↗
PubMed2000

Quantitative analysis of ammonia oxidising bacteria using competitive PCR.

Culture-based methods for enumeration, such as most probable number (MPN) methodologies, have proved inefficient due to difficulties in the isolation and cultivation of ammonia oxidising bacteria in the laboratory. Biases are associated with the isolation of bacteria in selective media and organisms cultivated in the laboratory may not be truly representative of those in the environment. In this study, we developed a competitive PCR (cPCR)-based method based on the amplification of 16S rRNA genes specific for the beta-subgroup proteobacterial ammonia oxidising bacteria for enumeration of these organisms. Populations in both agricultural soils and estuarine sediments were quantified by traditional MPN and by cPCR. The numbers of ammonia oxidisers for both sample types were significantly underestimated by conventional MPN and were 1-3 orders of magnitude lower than those obtained by cPCR. Higher numbers of ammonia oxidisers found in fertilised plots in agricultural soils by the cPCR technique were not observed in MPN estimates. It was necessary to construct a separate standard curve for each sample type as differences in DNA extraction, quantity and purity had a significant bearing on the ease of PCR of both competitor and target DNA.

Journal Article↗
PubMed2005

Oxidative addition of ammonia to form a stable monomeric amido hydride complex.

The insertion of an iridium complex into an N-H bond in ammonia leads to a stable monomeric amido hydride complex in solution at room temperature. This reaction advances the transition-metal coordination chemistry of ammonia beyond its role for more than a century as an ancillary ligand. The precursor for this insertion reaction is an iridium(I) olefin complex with an aliphatic ligand containing one carbon and two phosphorus donor atoms. Kinetic and isotopic labeling studies indicate that olefin dissociates to give a 14-electron iridium(I) fragment, which then reacts with ammonia. This cleavage of the N-H bond under neutral conditions provides a foundation on which to develop future mild catalytic transformations of ammonia, such as olefin hydroamination and arene oxidative amination.

Journal Article↗
PubMed1998

Loss of ammonia monooxygenase activity in nitrosomonas europaea upon exposure to nitrite

Nitrosomonas europaea, an obligate ammonia-oxidizing bacterium, lost an increasing amount of ammonia oxidation activity upon exposure to increasing concentrations of nitrite, the primary product of ammonia-oxidizing metabolism. The loss of activity was specific to the ammonia monooxygenase (AMO) enzyme, as confirmed by a decreased rate of NH4+-dependent O2 consumption, some loss of active AMO molecules observed by polypeptide labeling with 14C2H2, the protection of activity by substrates of AMO, and the requirement for copper. The loss of AMO activity via nitrite occurred under both aerobic and anaerobic conditions, and more activity was lost under alkaline than under acidic conditions except in the presence of large concentrations (20 mM) of nitrite. These results indicate that nitrite toxicity in N. europaea is mediated by a unique mechanism that is specific for AMO.

Journal Article↗
PubMed1990

Inhibition of ammonia monooxygenase in Nitrosomonas europaea by carbon disulfide.

Carbon disulfide has long been recognized as a potent inhibitor of nitrification, and it is the likely active component in several nitrification inhibitors suitable for field use. The effects of this compound on Nitrosomonas europaea have been investigated, and the site of action has been determined. Low concentrations of CS2 (less than 400 microM) produced a time-dependent inhibition of ammonia-dependent O2 uptake but did not inhibit hydrazine-oxidizing activity. CS2 also produced distinct changes in difference spectra of whole cells. These results suggest that ammonia monooxygenase (AMO) is the site of action of CS2. Unlike the case for thiourea and acetylene, saturating concentrations of CS2 did not fully inhibit AMO, and the inhibition resulted in a low but significant rate of ammonia-dependent O2 uptake. The effects of CS2 were not competitive with respect to ammonia concentration, and the inhibition by CS2 did not require the turnover of AMO to take effect. The ability of CS2-treated cells to incorporate [14C]acetylene into the 28-kilodalton polypeptide of AMO was used to demonstrate that the effects of CS2 are compatible with a mode of action which involves a reduction of the rate of turnover of AMO without effects on the catalytic mechanism. It is proposed that CS2 may act on AMO by reversibly reacting with a suitable nucleophilic amino acid in close proximity to the active site copper.

Acetylene↗
PubMed2002

Sensitivity improvement of ammonia determination based on flow-injection indophenol spectrophotometry with manganese(II) ion as a catalyst and analysis of exhaust gas of thermal power plant.

The sensitivity improvement of a flow-injection spectrophotometric method for the determination of ammonia was examined based on an indophenol blue coloration reaction with salicylate and hypochlorite in the presence of manganese(II) as a reaction promotion catalyst. The optimal conditions for achieving higher sensitivity of ammonia determination were examined using a three-line flow system. The limit of detection corresponding to a signal-to-noise ratio (S/N) of 3 was 0.005 mg l(-1) (approximately equal to 5 ppb) of NH4+. A calibration graph was linear in the range from 5 ppb to 1,000 ppb of ammonium ion. The relative standard deviations (n = 9) for 50 ppb and 100 ppb of ammonium ion were 6.4% and 2.2%, respectively. The proposed method was applied to the determination of ammonia in the exhaust gas of a thermal power plant. Prior to the FIA determination, ammonia in the exhaust gas was absorbed into a boric acid solution; the absorption solution was then analyzed by the proposed FIA.

Journal Article↗
PubMed1990

The effects of ammonia tolerance tests on the cerebrospinal fluid concentrations of amino acids and indoleamines in patients with liver cirrhosis.

To study the effect of ammonia administration on amino acids and indoleamines in cerebrospinal fluid (CSF) and on amino acids, insulin, and glucagon in plasma in humans with liver cirrhosis, we performed seven ammonia tolerance tests on six patients with stable liver cirrhosis. The grade of encephalopathy was determined by psychometric tests. Only one of the patients had pronounced encephalopathy. The other patients had no or only slight encephalopathy. The plasma concentrations of valine, leucine, isoleucine, phenylalanine, tyrosine, and methionine decreased after the ammonia load, whereas no changes were found in the plasma concentrations of glucagon and insulin. In CSF the concentrations of glutamine, aromatic amino acids, and indoleamines increased only in the patient who had pronounced encephalopathy, whereas no changes were found in the other patients. The effect of an ammonia load on the concentrations of neutral amino acids in CSF in patients with pronounced encephalopathy remains to be demonstrated.

5-Hydroxytryptophan↗
PubMed2005

[The characteristic state of health of ammonia nitrate producing workers].

The workers producing ammonia nitrate have professional contact with ammonia nitrate aerosol and nitrogenous gases. The state of health of ammonia producing workers has been examined. The morbidity, the therapeutic, neurological and laryngeal status have been inspected. Electrocardiography and examination by peak flow meter by Wotchall has been conducted. Peripheral blood test and radiography of backbone has been carried out as been required. It has been estimated that the illnesses of respiratory apparatus and musculoskeletal system predominate in the morbidity structure. The clinical examination of the workers with basic professions of the production of ammonia nitrate shows the frequent cases of chronic bronchitis and radiculoneuropathy. The results of function study show the damage of airways, the myocardiodystrophy and the changes of T wave. The nitrogen containing particulate pollutants that irritate respiratory systems and hard manual labor at these working places determine these illnesses. This fact corresponds with the hygiene and sanitary conditions of labor at major working places of production. This confirms the major role of occupational-productional factors in the etiology of these pathological conditions. In order to prevent the remote structural lesion of respiratory and cardiovascular systems it is required to amend the functional damage. On the basis of carefully performed study a complex of recreation measures has been carried out in order to improve the service conditions.

Female↗
PubMed1995

Effects of enhanced extracellular ammonia concentration on cultured mammalian retinal glial (Müller) cells.

Müller (glial) cells of the neonatal rabbit retina were cultured as confluent monolayers and exposed to enhanced concentrations of ammonia (0.25, 0.5, 1, 3, 7, and 10 mM) in medium for various periods (30 min to 10 d). This caused, in a time- and dose-dependent manner, similar changes in the Müller cells as had previously been described in cultured astrocytes. The most conspicuous events were 1) an increasing size of cell nuclei, 2) an accumulation of phagocytotic vacuoles, and 3) a rearrangement of intermediate filaments. 4) A considerable number of cells died when higher ammonia concentrations were applied for more than 1 h. Simultaneous application of dibutyryl-cyclic adenosine monophosphate (dBcAMP) prevented almost completely both the increase in cell nucleus size and the changes of intermediate filaments, but only partly the early cell death of a subpopulation of cells, and the accumulation of phagocytotic vacuoles. Further changes evoked by enhanced ammonia concentration were 5) an accumulation of lipofuscin-like material ("fatty degeneration") revealed by lipophilic stain, 6) reduced immunoreactivity for cathepsin D, and increased immunoreactivity for 7) glial fibrillary acidic protein, 8) glutamine synthetase, and 9) bcl-2 protooncogene protein. These findings are discussed in respect to the possible underlying pathophysiological mechanisms.

Ammonia↗
PubMed1992

The effect of various culture conditions on the levels of ammonia assimilatory enzymes of Corynebacterium callunae.

Corynebacterium callunae (NCIB 10338) grows faster on glutamate than ammonia when used as sole nitrogen sources. The levels of glutamine synthetase (GS; EC 6.3.1.2) and glutamate synthase (GOGAT; EC 1.4.1.13) of C. callunae were found to be influenced by the nitrogen source. Accordingly, the levels of GS and GOGAT activities were decreased markedly under conditions of ammonia excess and increased under low nitrogen conditions. In contrast, glutamate dehydrogenase (GDH; EC 1.4.1.4) activities were not significantly affected by the type or the concentration of the nitrogen source supplied. The carbon source in the growth medium could also affect GDH, GS and GOGAT levels. Of the carbon sources tested in the presence of 2 mM or 10 mM ammonium chloride as the nitrogen source pyruvate, acetate, fumarate and malate caused a decrease in the levels of all three enzymes as compared with glucose. GDH, GS and GOGAT levels were slightly influenced by aeration. Also, the enzyme levels varied with the growth phase. Methionine sulfoximine, an analogue of glutamine, markedly inhibited both the growth of C. callunae cells and the transferase activity of GS. The apparent Km values of GDH for ammonia and glutamate were 17.2 mM and 69.1 mM, respectively. In the NADPH-dependent reaction of GOGAT, the apparent Km values were 0.1 mM for alpha-ketoglutarate and 0.22 mM for glutamine.

Ammonia↗
PubMed1983

L-methionine-SR-sulfoximine as a probe for the role of glutamine synthetase in nitrogenase switch-off by ammonia and glutamine in Rhodopseudomonas palustris.

Methionine sulfoximine (MSX), an irreversible inhibitor of glutamine synthetase of Rhodopseudomonas palustris restored nitrogenase activity to cells in which nitrogenase had been completely inhibited by ammonia switch-off. After addition of MSX, there was a lag period before nitrogenase activity was fully restored. During this lag, glutamine synthetase activity progressively decreased, and near the time of its complete inhibition, nitrogenase activity resumed. Nitrogenase switch-off by ammonia thus required active glutamine synthetase. Glutamine itself caused nitrogenase inhibition whose reversal by MSX depended on the relative ratio of MSX to glutamine. Unlike ammonia, glutamine inhibited nitrogenase under conditions where glutamine synthetase activity was absent. This indicates that glutamine is the effector molecule in nitrogenase switch-off, for instance by interacting with the enzymatic system for Fe protein inactivation. The effects of glutamine and MSX were also dependent on the culture age. Possible explanation for this and for the competitive effects are a common binding site within the regulatory apparatus for nitrogenase, or, in part, within a common transport system. Some observations with MSX were extended to Rhodopseudomonas capsulata and agreed with those in R. palustris.

Ammonia↗
PubMed1991

Ammonia assimilation and glutamate incorporation in coenzyme F420 derivatives of Methanosarcina barkeri.

Methanosarcina barkeri was able to grow on L-alanine and L-glutamate as sole nitrogen sources. Cell yields were 0.5 g/l and 0.7 g/l (wet wt), respectively. The mechanism of ammonia assimilation in Methanosarcina barkeri strain MS was studied by analysis of enzyme activities. Activity levels of nitrogen-assimilating enzymes in extracts of cells grown on different nitrogen sources (ammonia, 0.05-100 mM; L-alanine, 10 mM; L-glutamate, 10 mM) were compared. Activities of glutamate dehydrogenase, glutamate synthase, glutamine synthetase, glutamate oxaloacetate transaminase and glutamate pyruvate transaminase could be measured in cells grown on these three nitrogen sources. Alanine dehydrogenase was not detected under the growth conditions used. None of the measured enzyme activities varied significantly in response to the NH4+ concentration. The length of the poly-gamma-glutamyl side chain of F420 derivatives turned out to be independent of the concentration of ammonia in the culture medium.

Alanine↗
PubMed1980

Properties of L-phenylalanine ammonia-lyase and turnover rate in etiolated and far-red illuminated seedlings of radish.

1. L-Phenylalanine ammonia-lyase (EC 4.3.1.5) was purified from radish cotyledons. The adsorption of the enzyme on L-phenylalanine-Sepharose 4B was nonspecific; the present data disprove the conclusions reached previously (Blondel, J.D., Huault, C., Faye, L., Rollin, P. and Cohen, P. (1973) FEBS Lett. 36, 239-244). 2. The apparent molecular weight of the enzyme fluctuated according to pH and ionic strength. A mean value of 290 000 was determined for the 'native' form. The activation energy was 54.4 kJ/mol. L- and D-phenylalanine protected the lyase from sodium borohydride denaturation. 3. Two Michaelis constants, KHm = 1.5 x 10(-5) M and KLm = 9.5 x 10(-5) M, were determined. The Hill coefficient value (h) was 0.48. This coefficient was 0.6 for cinnamate inhibition. These results suggest that phenylalanine ammonia-lyase in radish cotyledons is regulated by a negative cooperativity mechanism. 4. The phytochrome-mediated increase in phenylalanine ammonia-lyase activity was investigated by density labelling with 2H2O followed by isopycnic centrifugation in KBr gradients. An apparent half-life of 3.5 h was found for both the enzyme extracted from etiolated or far-red irradiated cotyledons. 5. Provided that phytochrome does not control the availability of labelled amino acids for protein synthesis, the present results are consistent with a far-red light-induced increase in the rate of synthesis of the lyase in radish cotyledons.

Ammonia-Lyases↗
PubMed1980

The mechanisms of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. Evidence that carbon-cobalt bond cleavage is driven in part by conformational alterations of the corrin ring.

Previous work has shown that the interaction between ethanolamine ammonia-lyase (ethanolamine ammonia-lyase, EC 4.3.1.7) and adenosylcobalamin weakens the C-Co bond of the cofactor with respect to homolytic cleavage. To obtain information concerning the mechanism by which this is accomplished, a study was conducted in which optical and circular dichroism spectroscopy were used to explore the interaction between ethanoloamine ammonia-lyase and a series of adenosylcobalamin analogs composed of an adenyl residue attached to the cobalt atom of cobalamin by a methylene chain whose length varies from 2 to 6 carbons. These studies indicated that the binding of a cobalamin to the active site activates forces which tend to alter the conformation of the enzyme, and with it that of the corrin ring, but that these conformational changes are blocked by bulky Co-beta substituents which restrict corrin ring flexibility. We postulate that at least one element of the force which weakens the C-Co bond of the enzyme-bound cofactor is the relief of conformational strain which occurs when C-Co bond cleavage, by releasing the interfering adenosyl group, permits the enzyme and the corrin ring to assume the energetically favored conformation.

Ammonia-Lyases↗