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PubMed1977

Spinach nitrite reductase. Purification and properties of a siroheme-containing iron-sulfur enzyme.

Ferredoxin-nitrite reductase (EC 1.7.7.1.) from spinach has been purified to homogeneity with a specific activity of 110 units/mg of protein. The enzyme, Mr = 61,000 has 3 iron atoms (of which one is in siroheme) and 2 labile sulfides, i.e. 1 (Fe2-S2) per molecule, with absorption maxima at 276, 386 (Soret), 573 (alpha), and 690 nm, with an E386 of 3.97 X 10(4) M-1-cm-1, and A276/A386 absorptivity ratio of 1.8. Anaerobic addition of dithionite results in the loss of the 690 nm peak and the splitting of the 573 nm absorption band into two broad peaks at 545 and 585 nm. Reduction by dithionite is enhanced by cyanide (Fig. 7) and requires about 3 electron eq per mol of enzyme. With nitrite or hydroxylamine (substrates of the enzyme), cyanide (a competitive inhibitor with respect to nitrite), or sulfite, the 690 nm absorption band of substrate-free enzyme disappears and the absorbance in the Soret and alpha region are altered. The high spin EPR signals disappear (J. M. Vega, H. Kamin, N. R. Orme-Johnson, and W. H. Orme-Johnson, unpublished observations). Titration permits calculation of 1 mol of nitrite bound/mol of enzyme with a Kdiss of 3.2 X 10(-6) M. Dithionite-reduced enzyme also forms complexes with added nitrite, hydroxylamine, or cyanide, characterized by marked alterations in the 573 (alpha) absorption band. THus, substrates or competitive inhibitors can be bound to the oxidized or reduced enzyme forms. CO inhibits nitrite reductase and forms a complex with reduced enzyme (epsilonmax at 395, 543, and 585 nm). Formation or dissociation of the spectrophotometrically detectable CO complex correlates with inhibition or inhibition-reversal of nitrite reduction catalysis. During steady state turnover with dithionite and nitrite, the enzyme forms a complex with added nitrite with absorption difference maxima at 445, 538, and 580 nm with respect to reduced enzyme. When nearly all substrate is depleted the spectrum of a new species appears, indicating that nitrite reductase may form complexes with nitrogen compounds of more than one oxidation state. Nitrite is stoichiometrically reduced to ammonia without detectable free nitrogen compounds of intermediate reduction state. p-Chloromercuribenzoate (pCMB) inhibits nitrite reductase activity and nitrite partially protects against this inhibition. Titration of native enzyme with the mercurial shows that 6 mol of pCMB can be bound/mol or nitrite reductase. The Soret absorption band of the native nitrite reductase is altered and partially bleached in the pCMB-treated enzyme, and the 573 (alpha) band disappears.

Amino Acids↗
PubMed1986

Identification of some polycyclic nitrogen-containing compounds in coal-derived oil.

A systematic method for the identification of aza-arenes in coal-derived oil was developed. The basic nitrogen-containing substances were extracted with 6 M hydrochloric acid and fractionated sequentially by using gel chromatography and thin-layer chromatography (TLC) on an alumina plate. The aza-arenes in these fractions were separated by using glass capillary gas chromatography. Individual compounds in the column effluent were trapped in a system consisting of a valve for flow switching and a trapping tube made from a glass capillary. The fluorescence spectra of nanogram to subnanogram amounts of trapped compounds were measured. Some attempts were made to identify components based on their TLC RF values and their fluorescence spectra, in addition to their mass spectra.

Aza Compounds↗
PubMed2006

Chemiluminescent method for detection of eutrophication sources by estimation of organic amino nitrogen and ammonium in water.

An automatic method has been developed for the estimation of organic amino nitrogen (CH2-NH) and ammonium in water samples. We propose a continuous flow system in which nitrogen compounds react with hypochlorite reagent to produce chloramines. Subsequently, the mixture is mixed with luminol, generating a chemiluminescence signal. The signal emission at 425 nm, registered as a function of time, decreases as nitrogen concentration increases, due to the decrease on hypochlorite concentration. A large number of nitrogen compounds have been assayed and their sensitivities compared, in milligrams per liter nitrogen. The ammonium calibration graph, expressed as N, can be used for most of the assayed compounds. The linear interval was 0.24-4 mg L(-1) N, with the detection limit 0.07 mg L(-1) N. The chemiluminescence method was applied to the analysis of several kinds of real water samples, natural, lake, irrigation ditch, fountain, residual, and seawater in order to detect possible sources of eutrophication. The accuracy (% relative error) and precision were satisfactory, with mean values of 5 +/- 4 and 3 +/- 2, respectively. This procedure has been used to estimate nitrogen content in samples before and after Kjeldahl treatment. In the same samples, the N found for the untreated samples provided a good estimation of the N Kjeldahl. Sixty samples per hour can be analyzed, and the procedure can also be used for in situ monitoring.

Journal Article↗
PubMed2001

Nitrogen metabolite repression in Hansenda polymorpha: the nmrl-l mutation.

In Hansenula polymorpha, the expression of the nitrate assimilation metabolism is subjected to re-pression-derepression mechanisms triggered by reduced nitrogen compounds such as ammonium. To further our knowledge on the genetics of these regulatory mechanisms, a screening strategy for the isolation of mutants exhibiting nitrate reductase activities in the presence of reduced nitrogen compounds was set up. This strategy makes use of a nitrate+ methylamine mutant to isolate suppressors of its characteristic phenotype--the inability to grow on a nitrate plus methylamine medium. A total of 21 regulatory mutants were isolated with this strategy and grouped into five complementation classes. One of these mutants harbours the recessive mutation nmr1-1, which determines the derepression of the nitrate assimilation metabolism in media containing nitrate plus a repressing nitrogen source (ammonium, methylamine, glutamate, urea or aspartate). Therefore, nitrate reductase activities are detected in the presence of reduced nitrogen sources, as long as nitrate is also in the medium. Our data indicate that the processes of repression-derepression and induction are controlled by elements which are distinct. Furthermore, they indicate that Nmrlp is involved in repressing circuits which control not only the nitrate-utilisation pathway, but also other pathways which are necessary for the utilisation of nitrogen sources alternative to ammonium. Of considerable interest is the fact that our nmr1-1 mutant is derepressed in glutamate but not in glutamine. Since the phenotype of this mutant seems to exclude a glutamine synthetase defect, we suggest that glutamate (or a derivative of this compound) might be involved in signalling nitrogen metabolite repression in H. polymorpha. Thus, in H. polymorpha, a glutamine-dependent circuit may co-exist with a glutamine-independent circuit.

Crosses, Genetic↗
PubMed1976

Diagnosis of disorders in amino acid methabolism by chemical ionization mass spectrometry.

A semi-quantitative method has been developed for rapid determination of amino acids and other nitrogenous compounds in human urine. The method uses direct chemical ionization mass spectrometry with isobutane as reagent. The nitrogenous compounds are separated from the urine samples by ion exchange. Disorders in amino acid metabolism have been determined by this method in patients suffering from phenylketonuria, cystinuria and maple-syrup urihe disease.

Amino Acids↗
PubMed2004

Nitrate reduction and the nitrogen cycle in archaea.

The nitrogen cycle (N-cycle) in the biosphere, mainly driven by prokaryotes, involves different reductive or oxidative reactions used either for assimilatory purposes or in respiratory processes for energy conservation. As the N-cycle has important agricultural and environmental implications, bacterial nitrogen metabolism has become a major research topic in recent years. Archaea are able to perform different reductive pathways of the N-cycle, including both assimilatory processes, such as nitrate assimilation and N(2) fixation, and dissimilatory reactions, such as nitrate respiration and denitrification. However, nitrogen metabolism is much less known in archaea than in bacteria. The availability of the complete genome sequences of several members of the eury- and crenarchaeota has enabled new approaches to the understanding of archaeal physiology and biochemistry, including metabolic reactions involving nitrogen compounds. Comparative studies reveal that significant differences exist in the structure and regulation of some enzymes involved in nitrogen metabolism in archaea, giving rise to important conclusions and new perspectives regarding the evolution, function and physiological relevance of the different N-cycle processes. This review discusses the advances that have been made in understanding nitrate reduction and other aspects of the inorganic nitrogen metabolism in archaea.

Archaea↗
PubMed1996

113Cd Shielding Tensors of Monomeric Cadmium Compounds Containing Nitrogen Donor Atoms. 3. CP/MAS Studies on Five-Coordinate Cadmium Complexes Having N(3)X(2) (X = H, N, O, and S) Donor Atoms.

The principal elements of the (113)Cd shielding tensor for a set of five- coordinate compounds having mixed donor atoms coordinating to the cadmium were determined via CP/MAS NMR experiments. The first complex, [HB(3,5-Me(2)pz)(3)]CdBH(4) (where pz = pyrazolyl), has a CdN(3)H(2) inner coordination sphere. The isotropic chemical shift in the solid state is 355.1 ppm, and its chemical shift anisotropy (CSA, Deltasigma) is -596 ppm with an asymmetry parameter (eta) of 0.64. The second complex, [HB(3,5-Me(2)pz)(3)]Cd[H(2)B(pz)(2)], has five nitrogen donor atoms bonded to the cadmium. This N(5) or N(3)N(2) compound was the only material of this study to manifest dipolar splitting of the cadmium resonance from the quadrupolar (14)N. The isotropic chemical shift, CSA, and the value of eta for this material were therefore determined at higher field where the dipolar splitting was less than the linewidth, yielding values of 226.6 ppm, -247 ppm, and 0.32, respectively. A second N(5) material, [HB(3-Phpz)(3)]Cd[H(2)B(3,5-Me(2)pz)(2)], was also investigated and has an isotropic shift of 190.2 ppm, a CSA of 254 ppm, and an eta of 0.86. Also studied was [HB(3-Phpz)(3)]Cd[(Bu(t)CO)(2)CH], which has an CdN(3)O(2) inner core. The isotropic chemical shift of this complex is 173.6 ppm, and the values of Deltasigma and eta were determined to be -258 ppm and 0.38, respectively. The final compound, [HB(3,5-Me(2)pz)(3)]Cd[S(2)CNEt(2)], with N(3)S(2) donor atoms, has an isotropic shift of 275.8 ppm, an eta of 0.51, and a CSA of +375 ppm. Utilizing previous assignments, the most shielded tensor element was determined to be oriented normal to the plane of the tridentate ligand. The shielding tensor information is used to speculate on the coordination geometry of the CdN(3)O(2) inner core complex.

Journal Article↗
PubMed2001

Structural requirements of benzodiazepines for the inhibition of pig brain nitric oxide synthase.

Nitric oxide synthases (NOS) are heme-containing enzymes which catalyse the oxidation of L-arginine to nitric oxide and L-citrulline. Some nitrogenated compounds have been reported to coordinate with the iron atom from the heme group, thus inhibiting NOS. 1,4-Benzodiazepines are nitrogenated compounds which have many physiological effects such as antianxiety, antiepileptic, hypnotic, and muscle relaxation properties. The aim of this paper was to measure the effect of different benzodiazepines on NOS activity in pig brain extracts. Medazepam, pinazepam, diazepam, oxazepam and alprazolam competitively inhibited NOS with IC(50) in the micromolar range. Other benzodiazepines showed no effect at concentrations as high as 200 microM. Due to the structural similarity of the benzodiazepine ring nucleus with L-arginine, we propose a benzodiazepine-enzyme interaction to explain the competitive inhibitions. By comparing benzodiazepine effects and their structures, the inhibitory effect of benzodiazepines on NOS is related to the absence of substituents on N4 and to the absence of a halogen substituent on C5 phenyl group. Although benzodiazepine's inhibitions observed in this study are not in the physiological range in normal cases, these inhibitions could be significant in drug abuse situations and should be taken into account for the rational design of drugs which specifically inhibit NOS.

Animals↗
PubMed2002

Method for determining nitrogenous heterocycle compounds in wine.

Qualitative and quantitative analyses of N-heterocycle compounds were conducted by using a liquid-liquid extraction followed by additional chemical silica gel purification and injection into a gas chromatographic (GC) column coupled to a nitrogen-phosphorus detector (NPD). The purified extract fraction was investigated by GC-NPD and by GC-mass spectrometry. The compounds identified and quantified in wines were 2,4,5-trimethyloxazole, 2,4-dimethylthiazole, and 4-methylthiazole by GC-NPD and both 2-acetylthiazole and 2-acetyl-2-thiazoline by GC-MS. The procedure was used to analyze different wines and gave reliable and reproducible results.

Chromatography, Gas↗
PubMed1963

Demonstration of increased permeability as a factor in the effect of acetylcholine on the electrical activty of venom-treated axons.

D-Tubocurarine (curare) and acetylcholine (ACh) had been found to block electrical activity after treatment of squid giant axons with cottonmouth moccasin venom at a concentration which had no effect on conduction. It has now been demonstrated that this effect is attributable to reduction of permeability barriers. The penetration of externally applied C(14)-labeled dimethylcurare, ACh, choline, and trimethylamine into the axoplasm of the squid giant axon was determined in axons treated with either cottonmouth, rattlesnake, or bee venom, and in untreated control axons. The lipid-soluble tertiary nitrogen compound trimethylamine readily penetrated into the axoplasm of untreated axons. In contrast, after exposure of the axons to the lipid-insoluble quaternary nitrogen compounds for 1 hour their presence in the axoplasm was hardly detectable (less than 1 per cent). However, following 15microg/ml cottonmouth venom 1 to 5 per cent of their external concentration is found within the axoplasm while following 50microg/ml venom 10 to 50 per cent enters. The penetration of dimethylcurare is also increased by 10 microg/ml bee venom but not by 1 microg/ml bee venom nor 1000 microg/ml rattlesnake venom. The experiments show that when ACh and curare, following venom treatment, affect electrical activity, they also penetrate into the axon. Treatments which do not increase penetration are also ineffective in rendering the compounds active.

Acetylcholine↗
PubMed1999

Transporters for ammonium, amino acids and peptides are expressed in pitchers of the carnivorous plant Nepenthes.

Insect capture and digestion contribute substantially to the nitrogen budget of carnivorous plants. In Nepenthes, insect-derived nitrogenous compounds are imported from the pitcher fluid and transported throughout the plant via the vascular tissue to support growth. Import and distribution of nutrients may require transmembrane nitrogen transporters. Representatives of three classes of genes encoding transporters for the nitrogenous compounds ammonium, amino acids and peptides were identified in Nepenthes pitchers. The expression at the cellular level of an ammonium transporter gene, three amino acid transporter genes, and one peptide transporter gene were investigated in the insect trapping organs of Nepenthes. Expression of the ammonium transporter gene NaAMT1 was detected in the head cells of digestive glands in the lower part of the pitcher where NaAMT1 may function in ammonium uptake from the pitcher fluid. One amino acid transporter gene, NaAAP1, was expressed in bundle sheath cells surrounding the vascular tissue. To understand the locations where transmembrane transport could be required within the pitcher, symplasmic and apoplasmic continuity was probed using fluorescent dyes. Symplasmic connections were not found between cortical cells and vascular bundles. Therefore, the amino acid transporter encoded by NaAAP1 may be involved in transport of amino acids into the vascular tissue. In contrast, expression of the peptide transporter gene NaNTR1 was detected in phloem cells of the vascular tissue within pitchers. NaNTR1 may function in the export of nitrogen from the pitcher by loading peptides into the phloem.

Amino Acid Sequence↗
PubMed1966

Chelation effects on Azotobacter cells and cysts.

Goldschmidt, Millicent C. (University of Texas, Austin), and Orville Wyss. Chelation effects on Azotobacter cells and cysts. J. Bacteriol. 91:120-124. 1966.-Ethylenediaminetetraacetate (EDTA) is very toxic to Azotobacter in the presence of nitrogen compounds that form complexes with it. This appears to be due to stronger chelation of certain metal ions by the complex. When such complexes of EDTA and nitrogen compound are absent, Azotobacter cysts can be ruptured by chelation without being killed. The lethal action as well as the cyst rupture is modified by the presence of salts.

Azotobacter↗