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PubMed2002

Leaf-atmosphere NH(3) exchange of white clover (Trifolium repens L.) in relation to mineral N nutrition and symbiotic N(2) fixation.

Plant-atmosphere NH(3) exchange was studied in white clover (Trifolium repens L. cv. Seminole) growing in nutrient solution containing 0 (N(2) based), 0.5 (low N) or 4.5 (high N) mM NO(3)(-). The aim was to show whether the NH(3) exchange potential is influenced by the proportion of N(2) fixation relative to NO(3)(-) supply. During the treatment, inhibition of N(2) fixation by NO(3)(-) was followed by in situ determination of total nitrogenase activity (TNA), and stomatal NH(3) compensation points (chi(NH(3))) were calculated on the basis of apoplastic NH4(+) concentration ([NH4(+)]) and pH. Whole-plant NH(3) exchange, transpiration and net CO(2) exchange were continuously recorded with a controlled cuvette system. Although shoot total N concentration increased with the level of mineral N application, tissue and apoplastic [NH4(+)] as well as chi(NH(3)) were equal in the three treatments. In NH(3)-free air, net NH(3) emission rates of <1 nmol m(-2) s(-1) were observed in both high-N and N(2)-based plants. When plants were supplied with air containing 40 nmol mol(-1) NH(3), the resulting net NH(3) uptake was higher in plants which acquired N exclusively from symbiotic N(2) fixation, compared to NO(3)(-) grown plants. The results indicate that symbiotic N(2) fixation and mineral N acquisition in white clover are balanced with respect to the NH4(+) pool leading to equal chi(NH(3)) in plants growing with or without NO(3)(-). At atmospheric NH(3) concentrations exceeding chi(NH(3)), the NH(3) uptake rate is controlled by the N demand of the plants.

Ammonia↗
PubMed1979

Active hydrogen by chemical ionization mass spectrometry.

A means of determination of a ctive hydrogen of hydroxyl, carboxyl, sulfhydryl, amino, amido and sulfonamido groups by chemical ionization mass spectrometry using ammonia and trideuterioammonia as reagent gases is described. The method is based on exchange of active hydrogen for deuterium occurring during the chemical ionization process using trideuterioammonia, with comparison of m/z for ammonium adduct [M + NH1]+ and trideuterioammonium adduct [M--nH + nD + ND4]+, or of protonated molecular ion [M + H]+ and deuteronated molecular ion [M--nH + nD + D]+ yielding the number of active hydrogens. Applications have been made to several classes of biologically important compounds.

Ammonia↗
PubMed1978

Structures and moelcular motions in alkaline earth hexammines.

The alkaline earth hexammines have novel structures and molecular motions. The ammonia molecules in these compounds adopt an entirely different geometry from that of normal ammonia. There are two motional transitions as the temperature is increased. The first transition is due to ammonia rotation, and the second results from ammonia diffusion.

Magnetic Resonance Spectroscopy↗
PubMed1981

Ammonia Assimilation in Alnus glutinosa and Glycine max: SHORT-TERM STUDIES USING [N]AMMONIUM.

The pattern of assimilation of NH(4) (+) by Alnus glutinosa, a N(2)-fixing, nonleguminous angiosperm, was examined. Detached nodules, roots, and nodulated roots of intact plants were exposed to (13)NH(4) (+) for up to 15 minutes. Glutamine was the most highly labeled compound at all times; the only other compound labeled significantly was glutamate. Similar results were obtained after incubating soybean (L. merr) nodules and roots with (13)NH(4) (+). These observations and the results of pulse-labeling and inhibitor studies with nodules of Alnus were distinctly different from those predicted for the assimilation of NH(4) (+) via glutamine synthetase and glutamate synthase and suggest that glutamate dehydrogenase may play a major role in the assimilation of exogenously supplied NH(4) (+).

Journal Article↗
PubMed1995

Selective, in vivo observation of [5-15N]glutamine amide protons in rat brain by 1H-15N heteronuclear multiple-quantum-coherence transfer NMR.

The amide protons of [5-15N]glutamine were selectively observed in vivo in the brains of anesthetized, spontaneously breathing rats after intravenous 15NH4+ infusion by 1H-15N heteronuclear multiple-quantum-coherence (HMQC) transfer NMR at 200 MHz for 1H. The peak intensity of the upfield amide proton was proportional to brain [5-15N]glutamine concentration. The 15N-decoupled amide-proton signal was observed in vivo in 2 min of acquisition at a brain [5-15N]glutamine concentration of 7.7 +/- 0.4 mumol/g, in < 8 min at 4.35 +/- 0.15 mumol/g, and in 17-34 min at 2.0 +/- 0.1 mumol/g. 1H signals not coupled to 15N were suppressed by phase cycling. The result suggests that 1H-15N HMQC will be useful for kinetic study of glutamine synthesis in rat brain in vivo at physiological concentrations of brain ammonia.

Amides↗
PubMed2003

Airborne reduced nitrogen: ammonia emissions from agriculture and other sources.

Ammonia is a basic gas and one of the most abundant nitrogen-containing compounds in the atmosphere. When emitted, ammonia reacts with oxides of nitrogen and sulfur to form particles, typically in the fine particle size range. Roughly half of the PM(2.5) mass in eastern United States is ammonium sulfate, according to the US EPA. Results from recent studies of PM(2.5) show that these fine particles are typically deposited deep in the lungs and may lead to increased morbidity and/or mortality. Also, these particles are in the size range that will degrade visibility. Ammonia emission inventories are usually constructed by multiplying an activity level by an experimentally determined emission factor for each source category. Typical sources of ammonia include livestock, fertilizer, soils, forest fires and slash burning, industry, vehicles, the oceans, humans, pets, wild animals, and waste disposal and recycling activities. Livestock is the largest source category in the United States, with waste from livestock responsible for about 3x10(9) kg of ammonia in 1995. Volatilization of ammonia from livestock waste is dependent on many parameters, and thus emission factors are difficult to predict. Despite a seasonal variation in these values, the emission factors for general livestock categories are usually annually averaged in current inventories. Activity levels for livestock are from the USDA Census of Agriculture, which does not give information about animal raising practices such as housing types and grazing times, waste handling systems, and approximate animal slurry spreading times or methods. Ammonia emissions in the United States in 1995 from sources other than livestock are much lower; for example, annual emissions are roughly 8x10(8) kg from fertilizer, 7x10(7) kg from industry, 5x10(7) kg from vehicles and 1x10(8) kg from humans. There is considerable uncertainty in the emissions from soil and vegetation, although this category may also be significant. Recommendations for future directions in ammonia research include designing experiments to improve emission factors and their resolution in all significant source categories, developing mass balance models, and refining of the livestock activity level data by eliciting judgment from experts in this field.

Agriculture↗
PubMed1983

Cysteine conjugate beta-lyase in the gastrointestinal bacterium Fusobacterium necrophorum.

A cysteine conjugate beta-lyase from the anaerobic gastrointestinal bacterium Fusobacterium necrophorum was purified 51-fold by heat treatment, ammonium sulphate fractionation, gel-filtration chromatography, and anion-exchange chromatography. This enzyme catalyses the cleavage of the thioether linkage in cysteine conjugates of the following S-alkyl- or S-aryl-linked compounds: cysteine conjugate of propachlor (2-S-cysteinyl-N-isopropylacetanilide); 1,2-dihydro-1-hydroxy-2-S-cysteinylnaphthalene and S-(2-benzothiazolyl)cysteine. 2-Mercapto-N-isopropylacetanilide, pyruvic acid and ammonia were produced from the beta-lyase cleavage of the cysteine conjugate of propachlor in equimolar ratios. The apparent Km values for the cysteine conjugate of propachlor and S-(benzothiazolyl)cysteine were 1.1 and 1.0 mM, respectively. Pyridoxal phosphate was required for enzymic activity. Ammonium ion activated enzymic activity, while hydroxylamine completely inhibited the enzyme. Dithiothreitol and bovine serum albumin had no effect on enzymic activity.

Carbon-Sulfur Lyases↗
PubMedDate not supplied

A 15N NMR study of in vivo cerebral glutamine synthesis in hyperammonemic rats.

Rats were given intravenous 15NH4+ infusion at a rate of 2.2 or 5.5 mmol/h/kg body wt to induce hyperammonemia, as animal models of hepatic encephalopathy. Its effect on cerebral amino acid metabolism was studied in vivo by 15N NMR spectroscopy at 20.27 MHz for 15N. Cerebral [gamma-15N]glutamine (present at a tissue concentration of 4-9 mumol/g) and [alpha-15N]glutamate/glutamine (6 mumol/g) were clearly observed in living rats within 9-18 min. In portacaval-shunted rats, final cerebral [gamma-15N]glutamine concentrations were higher than those in controls after the same infusion period, presumably because decreased 15NH4+ removal in the liver led to increased 15NH3 diffusion into the astrocytes. In control rats, cerebral [gamma-15N]glutamine pool increased at a rate of 1.7 mumol/h/g when blood ammonia concentration was 0.8 mM. 15N enrichment in gamma-15N was 71%. From these observations, in vivo activity of glutamine synthetase in rat brain was estimated to be 3.5 mumol/h/g. Comparison with reported optimum in vitro activity suggests that in situ concentrations of some substrates and cofactors limit the activity of glutamine synthetase in vivo.

Ammonia↗
PubMed2002

Physiological alterations and regulation of heterocyst and nitrogenase formation in Het(-) Fix(-) mutant strain of Anabaena variabilis.

Physiological alterations and regulation of heterocyst and nitrogenase formation have been studied in Het(-) Fix(-) mutant strain of diazotrophic cyanobacterium Anabaena variabilis. Het(-) Fix(-) mutant strain of A. variabilis has been isolated by N-methyl-N'-nitro-N"-nitrosoguanidine (NTG) mutagenesis and was screened with the penicillin enrichment (500 microg ml(-1)). Growth, heterocyst differentiation, nitrogenase and glutamine synthetase (biosynthetic and transferase), (14)CO(2)-fixation, nitrate reductase (NR), nitrite reductase (NiR), glucose-6-phosphate dehydrogenase (G6PDH), and isocitrate dehydrogenase (IDH) activities, and NO(3)(-), NO(2)(-), and NH(4)(+) uptake and whole cell protein profile in different metabolic conditions were studied in the Het(-) Fix(-) mutant strain taking wild-type A. variabilis as reference. Het(-) Fix(-) mutant strain was incapable of assimilating elemental nitrogen (N(2)) due to its inability to form heterocysts and nitrogenase and this was the reason for its inability to grow in BG-11(0) medium (free from combined nitrogen). In contrast, wild-type strain grew reasonably well in the absence of combined nitrogen sources and also showed heterocyst differentiation (8.5%) and nitrogenase activity (10.8 etamol C(2)H(4) formed microg(-1) Chl a h(-1)) in N(2)-medium. Wild-type strain also exhibited higher NR, NiR, and GS activities compared to its Het(-) Fix(-) mutant strain, which may presumably be due to acquisition of high uptake of NO(3)(-), NO(2)(-), and NH(2)(+). Wild-type strain in contrast to its Het(-) Fix(-) mutant strain also exhibited high level of G6PDH, IDH, and (14)CO(2) fixation activities. Low levels of G6PDH and IDH activities in Het(-) Fix(-) mutant strain further confirmed the lack of heterocyst differentiation and nitrogenase activity in the Het(-) Fix(-) mutant strain.NR, NiR, and GS activities in both the strains were energy-dependent and the energy required is mainly derived from photophosphorylation. Furthermore, it was found that de novo protein synthesis is necessarily required for the activities of NR, NiR, and GS in both wild-type and its Het(-) Fix(-) mutant strain.

Anabaena↗
PubMed1982

Ammonium (methylammonium) transport by Klebsiella pneumoniae.

Klebsiella pneumoniae can accumulate methylammonium up to 80-fold by means of a transport system as indicated by the energy requirement, saturation kinetics and a narrow pH profile around pH 6.8. Methylammonium transport (apparent Km = 100 microM, V = 40 mumol/min per g dry weight at 15 degrees C) is competitively inhibited by ammonium (apparent Ki = 7 microM). The low Ki value and the finding that methylammonium cannot serve as a nitrogen source indicate that ammonium rather than methylammonium is the natural substrate. Uphill transport is driven by a component of the protonmotive force, probably the membrane potential. The transport system is under genetic control; it is partially repressed by amino acids and completely by ammonium. Analysis of mutants suggest that the synthesis of the ammonium transport system is subject to the same 'nitrogen control' as nitrogenase and glutamine synthetase.

Ammonia↗
PubMed1995

In vivo activity of glutaminase in the brain of hyperammonaemic rats measured by 15N nuclear magnetic resonance.

The in vivo activity of phosphate-activated glutaminase (PAG) was measured in the brain of hyperammonaemic rat by 15N n.m.r. Brain glutamine was 15N-enriched by intravenous infusion of 15NH4+ until the concentration of [5-15N]glutamine reached 6.1 mumol/g. Further glutamine synthesis was inhibited by intraperitoneal injection of methionine-DL-sulphoximine, an inhibitor of glutamine synthetase, and the infusate was changed to 14NH4+ during observation of decrease in brain [5-15N]glutamine due to PAG and other glutamine utilization pathways. Progressive decrease in brain [5-15N]glutamine, PAG-catalysed production of 15NH4+ and its subsequent assimilation into glutamate by glutamate dehydrogenase were monitored in vivo by 15N n.m.r. Brain [5-15N]glutamine (15N enrichment of 0.35-0.50) decreased at a rate of 1.2 mumol/h per g of brain. The in vivo PAG activity, determined from the observed rate and the quantity of 15NH4+ produced and subsequently assimilated into glutamate and aspartate, was 0.9-1.3 mumol/h per g. This activity is less than 1.1% of the reported activity in vitro measured in rat brain homogenate at a 10 mM concentration of the activator Pi. Inhibition by ammonia (brain level 1.4 mumol/g) alone does not account for the observed low activity in vivo. The result strongly suggests that, in intact brain, PAG activity is maintained at a low level by a suboptimal in situ concentration of Pi and the strong inhibitory effect of glutamate. The observed PAG activity in vivo is lower than the reported in vivo activity of glutamate decarboxylase which converts glutamate into gamma-aminobutyrate (GABA). The result suggests that PAG-catalysed hydrolysis of glutamine is not the sole provider of glutamate used for GABA synthesis.

Ammonia↗
PubMed1972

Ammonia intoxication in rats: protection by N-carbamoyl-L-glutamate plus L-arginine.

Rats given a lethal dose (LD(99.9)) of ammonium acetate (10.8 mmol/kg of body weight) were protected to the extent of 85 and 76% when previously injected with N-carbamoyl glutamate or L-arginine, respectively, at a level of 4 mmol/kg of body weight. At a dose of 1 mmol/kg of body weight, L-arginine protected 24%, while N-carbamoyl-L-glutamate protected 61% of the animals. When a combination of N-carbamoyl-L-glutamate plus L-arginine (1 mmol each per kg of body weight) was injected, 100% of the rats were protected. The efficacy of N-carbamoyl-L-glutamate is related to its role as an activator of mitochondrial carbamoyl phosphate synthetase (EC 2.7.2.5) and its resistance to hydrolysis by tissue acylaminoacid acylase. N-Acetyl-L-glutamate, the naturally occurring and most effective activator of mitochondrial carbamoyl phosphate synthetase, was relatively ineffective in protection against lethal dose of ammonium acetate, because of its ready hydrolysis by acylaminoacid acylase. The findings reported provide a rational basis for the use of N-carbamoyl-L-glutamate plus L-arginine in the prevention and treatment of hyperammonemia in clinical conditions of liver disease and parental infusion of amino acids, and in feeding of urea supplements to ruminants.

Acetates↗
PubMed2004

Arabidopsis thaliana GLN2-encoded glutamine synthetase is dual targeted to leaf mitochondria and chloroplasts.

In higher plants, photorespiratory Gly oxidation in leaf mitochondria yields ammonium in large amounts. Mitochondrial ammonium must somehow be recovered as glutamate in chloroplasts. As the first step in that recovery, we report glutamine synthetase (GS) activity in highly purified Arabidopsis thaliana mitochondria isolated from light-adapted leaf tissue. Leaf mitochondrial GS activity is further induced in response to either physiological CO(2) limitation or transient darkness. Historically, whether mitochondria are fully competent for oxidative phosphorylation in actively photorespiring leaves has remained uncertain. Here, we report that light-adapted, intact, leaf mitochondria supplied with Gly as sole energy source are fully competent for oxidative phosphorylation. Purified intact mitochondria efficiently use Gly oxidation (as sole energy, NH(3), and CO(2) source) to drive conversion of l-Orn to l-citrulline, an ATP-dependent process. An A. thaliana genome-wide search for nuclear gene(s) encoding mitochondrial GS activity yielded a single candidate, GLN2. Stably transgenic A. thaliana ecotype Columbia plants expressing a p35S::GLN2::green fluorescent protein (GFP) chimeric reporter were constructed. When observed by laser scanning confocal microscopy, leaf mesophyll and epidermal tissue of transgenic plants showed punctate GFP fluorescence that colocalized with mitochondria. In immunoblot experiments, a 41-kD chimeric GLN2::GFP protein was present in both leaf mitochondria and chloroplasts of these stably transgenic plants. Therefore, the GLN2 gene product, heretofore labeled plastidic GS-2, functions in both leaf mitochondria and chloroplasts to faciliate ammonium recovery during photorespiration.

Amino Acid Sequence↗
PubMed1995

Effect of an ntrBC mutation on the posttranslational regulation of nitrogenase activity in Rhodospirillum rubrum.

Homologs of ntrB and ntrC genes from Rhodospirillum rubrum were cloned and sequenced. A mutant lacking ntrBC was constructed, and this mutant has normal nitrogenase activity under nif-derepressing conditions, indicating that ntrBC are not necessary for the expression of the nif genes in R. rubrum. However, the post-translational regulation of nitrogenase activity by ADP-ribosylation in response to NH4+ was partially abolished in this mutant. More surprisingly, the regulation of nitrogenase activity in response to darkness was also affected, suggesting a physiological link between the ntr system and energy signal transduction in R. rubrum. The expression of glutamine synthetase, as well as its posttranslational regulation, was also altered in this ntrBC mutant.

ADP Ribose Transferases↗