Nitrite Reductases
Nitrites
Salts of nitrous acid or compounds containing the group NO2-. The inorganic nitrites of the type MNO2 (where M=metal) are all insoluble, except the alkali nitrites. The organic nitrites may be isomeric, but not identical with the corresponding nitro compounds. (Grant & Hackh's Chemical Dictionary, 5th ed)
Nitrite Reductase (NAD(P)H)
Sodium Nitrite
Nitrous acid sodium salt. Used in many industrial processes, in meat curing, coloring, and preserving, and as a reagent in ANALYTICAL CHEMISTRY TECHNIQUES. It is used therapeutically as an antidote in cyanide poisoning. The compound is toxic and mutagenic and will react in vivo with secondary or tertiary amines thereby producing highly carcinogenic nitrosamines.
Ferredoxin-Nitrite Reductase
Nitrates
Cytochromes a1
Nitrate Reductase
Alcaligenes
Alcaligenes faecalis
NADH, NADPH Oxidoreductases
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
Oxidoreductases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Bacteroidaceae
Denitrification
Cytochromes c1
Azurin
A bacterial protein from Pseudomonas, Bordetella, or Alcaligenes which operates as an electron transfer unit associated with the cytochrome chain. The protein has a molecular weight of approximately 16,000, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308nm.
Oxidation-Reduction
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Cytochromes
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
Hydroxymethylglutaryl CoA Reductases
Heme
Anaerobiosis
Cytochrome-B(5) Reductase
A FLAVOPROTEIN oxidoreductase that occurs both as a soluble enzyme and a membrane-bound enzyme due to ALTERNATIVE SPLICING of a single mRNA. The soluble form is present mainly in ERYTHROCYTES and is involved in the reduction of METHEMOGLOBIN. The membrane-bound form of the enzyme is found primarily in the ENDOPLASMIC RETICULUM and outer mitochondrial membrane, where it participates in the desaturation of FATTY ACIDS; CHOLESTEROL biosynthesis and drug metabolism. A deficiency in the enzyme can result in METHEMOGLOBINEMIA.
Nitric Oxide
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
Copper
Electron Transport
Nitrosomonas europaea
Paracoccus pantotrophus
Spectrophotometry
Glutathione Reductase
FMN Reductase
Thioredoxin-Disulfide Reductase
Nitrous Oxide
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
NADPH-Ferrihemoprotein Reductase
Ferredoxins
Ferredoxin-NADP Reductase
Hydroxylamine
Wolinella
Amyl Nitrite
Electron Spin Resonance Spectroscopy
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
Cytochrome c Group
Ectothiorhodospiraceae
Pseudomonas
Amino Acid Sequence
Hyphomicrobium
A genus of rod-shaped, oval, or bean-shaped bacteria found in soil and fresh water. Polar prosthecae are present and cells reproduce by budding at the tips of the prosthecae. Cells of this genus are aerobic and grow best with one-carbon compounds. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Sulfite Reductase (Ferredoxin)
Electron Transport Complex IV
A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.
Pseudomonas aeruginosa
Ralstonia pickettii
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Tetrahydrofolate Dehydrogenase
An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.
Desulfovibrio
Nitrosomonas
Oxidoreductases Acting on Sulfur Group Donors
Nitrogen
Gene Expression Regulation, Bacterial
Quaternary Ammonium Compounds
Achromobacter denitrificans
The type species of gram negative, aerobic bacteria in the genus ACHROMOBACTER. Previously in the genus ALCALIGENES, the classification and nomenclature of this species has been frequently emended. The two subspecies, Achromobacter xylosoxidans subsp. denitrificans and Achromobacter xylosoxidans subsp. xylosoxidans are associated with infections.
Base Sequence
Methylenetetrahydrofolate Reductase (NADPH2)
Ammonia
Spectrum Analysis
Nitrate Reductase (NADH)
NADP
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
Iron-Sulfur Proteins
Pulse Radiolysis
Hemeproteins
Methionine Sulfoxide Reductases
Hydroxymethylglutaryl-CoA Reductase Inhibitors
Ribonucleoside Diphosphate Reductase
Mutation
Binding Sites
Sequence Homology, Amino Acid
Hydrogen-Ion Concentration
Dihydropteridine Reductase
Cytochromes c2
Rhodobacter sphaeroides
Oxygen
Cloning, Molecular
Quinone Reductases
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
Metalloproteins
Sequence Analysis, DNA
Electrons
Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.
Alcohol Oxidoreductases
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
Oxidoreductases Acting on CH-CH Group Donors
Flavins
Catalysis
Paraquat
Bacteria
One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.
Models, Molecular
Carbon Monoxide
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)
Dianisidine
Chromatiaceae
Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
Viologens
Crystallography, X-Ray
Hemoglobins
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Denitrifying Pseudomonas aeruginosa: some parameters of growth and active transport. (1/435)
Optimal cell yield of Pseudomonas aeruginosa grown under denitrifying conditions was obtained with 100 mM nitrate as the terminal electron acceptor, irrespective of the medium used. Nitrite as the terminal electron acceptor supported poor denitrifying growth when concentrations of less than 15 mM, but not higher, were used, apparently owing to toxicity exerted by nitrite. Nitrite accumulated in the medium during early exponential phase when nitrate was the terminal electron acceptor and then decreased to extinction before midexponential phase. The maximal rate of glucose and gluconate transport was supported by 1 mM nitrate or nitrite as the terminal electron acceptor under anaerobic conditions. The transport rate was greater with nitrate than with nitrite as the terminal electron acceptor, but the greatest transport rate was observed under aerobic conditions with oxygen as the terminal electron acceptor. When P. aeruginosa was inoculated into a denitrifying environment, nitrate reductase was detected after 3 h of incubation, nitrite reductase was detected after another 4 h of incubation, and maximal nitrate and nitrite reductase activities peaked together during midexponential phase. The latter coincided with maximal glucose transport activity. (+info)Molecular characterization of the nitrite-reducing system of Staphylococcus carnosus. (2/435)
Characterization of a nitrite reductase-negative Staphylococcus carnosus Tn917 mutant led to the identification of the nir operon, which encodes NirBD, the dissimilatory NADH-dependent nitrite reductase; SirA, the putative oxidase and chelatase, and SirB, the uroporphyrinogen III methylase, both of which are necessary for biosynthesis of the siroheme prosthetic group; and NirR, which revealed no convincing similarity to proteins with known functions. We suggest that NirR is essential for nir promoter activity. In the absence of NirR, a weak promoter upstream of sirA seems to drive transcription of sirA, nirB, nirD, and sirB in the stationary-growth phase. In primer extension experiments one predominant and several weaker transcription start sites were identified in the nir promoter region. Northern blot analyses indicated that anaerobiosis and nitrite are induction factors of the nir operon: cells grown aerobically with nitrite revealed small amounts of full-length transcript whereas cells grown anaerobically with or without nitrite showed large amounts of full-length transcript. Although a transcript is detectable, no nitrite reduction occurs in cells grown aerobically with nitrite, indicating an additional oxygen-controlled step at the level of translation, enzyme folding, assembly, or insertion of prosthetic groups. The nitrite-reducing activity expressed during anaerobiosis is switched off reversibly when the oxygen tension increases, most likely due to competition for electrons with the aerobic respiratory chain. Another gene, nirC, is located upstream of the nir operon. nirC encodes a putative integral membrane-spanning protein of unknown function. A nirC mutant showed no distinct phenotype. (+info)The GATA factor AreA is essential for chromatin remodelling in a eukaryotic bidirectional promoter. (3/435)
The linked niiA and niaD genes of Aspergillus nidulans are transcribed divergently. The expression of these genes is subject to a dual control system. They are induced by nitrate and repressed by ammonium. AreA mediates derepression in the absence of ammonium and NirA supposedly mediates nitrate induction. Out of 10 GATA sites, a central cluster (sites 5-8) is responsible for approximately 80% of the transcriptional activity of the promoter on both genes. We show occupancy in vivo of site 5 by the AreA protein, even under conditions of repression. Sites 5-8 are situated in a pre-set nucleosome-free region. Under conditions of expression, a drastic nucleosomal rearrangement takes place and the positioning of at least five nucleosomes flanking the central region is lost. Remodelling is strictly dependent on the presence of an active areA gene product, and independent from the NirA-specific and essential transcription factor. Thus, nucleosome remodelling is independent from the transcriptional activation of the niiA-niaD promoter. The results presented cast doubts on the role of NirA as the unique transducer of the nitrate induction signal. We demonstrate, for the first time in vivo, that a GATA factor is involved directly in chromatin remodelling. (+info)Nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells. (4/435)
We have recently reported that nitrite reductase, a bifunctional enzyme located in the periplasmic space of Pseudomonas aeruginosa, could induce interleukin-8 (IL-8) generation in a variety of respiratory cells, including bronchial epithelial cells (K. Oishi et al. Infect. Immun. 65:2648-2655, 1997). In this report, we examined the mode of nitrite reductase (PNR) release from a serum-sensitive strain of live P. aeruginosa cells during in vitro treatment with four different antimicrobial agents or human complement. Bacterial killing of P. aeruginosa by antimicrobial agents induced PNR release and mediated IL-8 production in human bronchial epithelial (BET-1A) cells. Among these agents, imipenem demonstrated rapid killing of P. aeruginosa as well as rapid release of PNR and resulted in the highest IL-8 production. Complement-mediated killing of P. aeruginosa was also associated with PNR release and enhanced IL-8 production. The immunoprecipitates of the aliquots of bacterial culture containing imipenem or complement with anti-PNR immunoglobulin G (IgG) induced twofold-higher IL-8 production than did the immunoprecipitates of the aliquots of bacterial culture with a control IgG. These pieces of evidence confirmed that PNR released in the aliquots of bacterial culture was responsible for IL-8 production in the BET-1A cells. Furthermore, the culture supernatants of the BET-1A cells stimulated with aliquots of bacterial culture containing antimicrobial agents or complement similarly mediated neutrophil migration in vitro. These data support the possibility that a potent inducer of IL-8, PNR, could be released from P. aeruginosa after exposure to antimicrobial agents or complement and contributes to neutrophil migration in the airways during bronchopulmonary infections with P. aeruginosa. (+info)PCR detection of genes encoding nitrite reductase in denitrifying bacteria. (5/435)
Using consensus regions in gene sequences encoding the two forms of nitrite reductase (Nir), a key enzyme in the denitrification pathway, we designed two sets of PCR primers to amplify cd1- and Cu-nir. The primers were evaluated by screening defined denitrifying strains, denitrifying isolates from wastewater treatment plants, and extracts from activated sludge. Sequence relationships of nir genes were also established. The cd1 primers were designed to amplify a 778 to 799-bp region of cd1-nir in the six published sequences. Likewise, the Cu primers amplified a 473-bp region in seven of the eight published Cu-nir sequences. Together, the two sets of PCR primers amplified nir genes in nine species within four genera, as well as in four of the seven sludge isolates. The primers did not amplify genes of nondenitrifying strains. The Cu primers amplified the expected fragment in all 13 sludge samples, but cd1-nir fragments were only obtained in five samples. PCR products of the expected sizes were verified as nir genes after hybridization to DNA probes, except in one case. The sequenced nir fragments were related to other nir sequences, demonstrating that the primers amplified the correct gene. The selected primer sites for Cu-nir were conserved, while broad-range primers targeting conserved regions of cd1-nir seem to be difficult to find. We also report on the existence of Cu-nir in Paracoccus denitrificans Pd1222. (+info)The blue copper-containing nitrite reductase from Alcaligenes xylosoxidans: cloning of the nirA gene and characterization of the recombinant enzyme. (6/435)
The nirA gene encoding the blue dissimilatory nitrite reductase from Alcaligenes xylosoxidans has been cloned and sequenced. To our knowledge, this is the first report of the characterization of a gene encoding a blue copper-containing nitrite reductase. The deduced amino acid sequence exhibits a high degree of similarity to other copper-containing nitrite reductases from various bacterial sources. The full-length protein included a 24-amino-acid leader peptide. The nirA gene was overexpressed in Escherichia coli and was shown to be exported to the periplasm. Purification was achieved in a single step, and analysis of the recombinant Nir enzyme revealed that cleavage of the signal peptide occurred at a position identical to that for the native enzyme isolated from A. xylosoxidans. The recombinant Nir isolated directly was blue and trimeric and, on the basis of electron paramagnetic resonance spectroscopy and metal analysis, possessed only type 1 copper centers. This type 2-depleted enzyme preparation also had a low nitrite reductase enzyme activity. Incubation of the periplasmic fraction with copper sulfate prior to purification resulted in the isolation of an enzyme with a full complement of type 1 and type 2 copper centers and a high specific activity. The kinetic properties of the recombinant enzyme were indistinguishable from those of the native nitrite reductase isolated from A. xylosoxidans. This rapid isolation procedure will greatly facilitate genetic and biochemical characterization of both wild-type and mutant derivatives of this protein. (+info)Bacterial nitric oxide synthesis. (7/435)
The structure-function relationships in nitrite reductases, key enzymes in the dissimilatory denitrification pathway which reduce nitrite to nitric oxide (NO), are reviewed in this paper. The mechanisms of NO production are discussed in detail and special attention is paid to new structural information, such as the high resolution structure of the copper- and heme-containing enzymes from different sources. Finally, some implications relevant to regulation of the steady state levels of NO in denitrifiers are presented. (+info)Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase? (8/435)
The structures of nitrite reductase from Paracoccus denitrificans GB17 (NiR-Pd) and Pseudomonas aeruginosa (NiR-Pa) have been described for the oxidized and reduced state (Fulop, V., Moir, J. W. B., Ferguson, S. J., and Hajdu, J. (1995) Cell 81, 369-377; Nurizzo, D., Silvestrini, M. C., Mathieu, M., Cutruzzola, F., Bourgeois, D., Fulop, V., Hajdu, J., Brunori, M., Tegoni, M., and Cambillau, C. (1997) Structure 5, 1157-1171; Nurizzo, D., Cutruzzola, F., Arese, M., Bourgeois, D., Brunori, M., Cambillau, C. , and Tegoni, M. (1998) Biochemistry 37, 13987-13996). Major conformational rearrangements are observed in the extreme states although they are more substantial in NiR-Pd. The four structures differ significantly in the c heme domains. Upon reduction, a His17/Met106 heme-ligand switch is observed in NiR-Pd together with concerted movements of the Tyr in the distal site of the d1 heme (Tyr10 in NiR-Pa, Tyr25 in NiR-Pd) and of a loop of the c heme domain (56-62 in NiR-Pa, 99-116 in NiR-Pd). Whether the reduction of the c heme, which undergoes the major rearrangements, is the trigger of these movements is the question addressed by our study. This conformational reorganization is not observed in the partially reduced species, in which the c heme is partially or largely (15-90%) reduced but the d1 heme is still oxidized. These results suggest that the d1 heme reduction is likely to be responsible of the movements. We speculate about the mechanistic explanation as to why the opening of the d1 heme distal pocket only occurs upon electron transfer to the d1 heme itself, to allow binding of the physiological substrate NO2- exclusively to the reduced metal center. (+info)
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1 Cytochromes-C-Reduced[c] + 1 NITRITE[c] + 2 PROTON[c] =, 1 Cytochromes-C-Oxidized[c] + 1 NITRIC-OXIDE[c] + 1 WATER[c] ... PWY-6523, nitrite-dependent anaerobic methane oxidation: *1 reactions found over 3 reactions in the full pathway ... Retrieved from "http://gem-aureme.genouest.org//cokagem/index.php?title=NITRITE-REDUCTASE-CYTOCHROME-RXN&oldid=6022" ...
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Complete genome sequence and comparative analysis of Shewanella violacea, a psychrophilic and piezophilic bacterium from deep...
Transporters and assimilatory reductases for nitrate and nitrite, and nitric oxide-detoxifying mechanisms (flavohemoglobin and ... Transporters and assimilatory reductases for nitrate and nitrite, and nitric oxide-detoxifying mechanisms (flavohemoglobin and ... Transporters and assimilatory reductases for nitrate and nitrite, and nitric oxide-detoxifying mechanisms (flavohemoglobin and ... Transporters and assimilatory reductases for nitrate and nitrite, and nitric oxide-detoxifying mechanisms (flavohemoglobin and ...
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This is an extensively derivatised heme; a comparison is drawn with another type of respiratory nitrite reductase in which the ... In contrast to the widespread c-type cytochromes, the d1 heme is restricted to a single enzyme, the cytochrome cd1 nitrite ... reductase that catalyses the one-electron reduction of nitrite to nitric oxide. ... the cytochrome cd1 nitrite reductase that catalyses the one-electron reduction of nitrite to nitric oxide. This is an ...
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Dissecting the role of NtrC and RpoN in the expression of assimilatory nitrate and nitrite reductases in Bradyrhizobium ... Development and application of an electronic tongue for detection and monitoring of nitrate, nitrite and ammonium levels in ... nitrite and ammonium in water. The electronic tongue was composed of an ... ...
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Dissecting the role of NtrC and RpoN in the expression of assimilatory nitrate and nitrite reductases in Bradyrhizobium ... Development and application of an electronic tongue for detection and monitoring of nitrate, nitrite and ammonium levels in ... nitrite and ammonium in water. The electronic tongue was composed of an ... ...
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periplasmic nitrate (or nitrite) reductase c-type cytochrome, NapC/NirT family 49.46 ... periplasmic nitrate (or nitrite) reductase c-type cytochrome, NapC/NirT family 43.32 ... periplasmic nitrate (or nitrite) reductase c-type cytochrome, NapC/NirT family 42.78 ... periplasmic nitrate (or nitrite) reductase c-type cytochrome, NapC/NirT family 42.25 ...
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Complete circular genome sequence and temperature independent adaptation to anaerobiosis of Listeria weihenstephanensis DSM...
SAUSA300 RS13990 - AureoWiki
Metabolism Central intermediary metabolism Nitrogen metabolism nitrite reductase [NAD(P)H], large subunit (TIGR02374; EC 1.7. ... putative selenate reductase, YgfK subunit (TIGR03315; HMM-score: 17.9) Metabolism Energy metabolism Amino acids and amines ... Metabolism Energy metabolism Electron transport thioredoxin-disulfide reductase (TIGR01292; EC 1.8.1.9; HMM-score: 32.3) ... Cellular processes Cellular processes Detoxification mercury(II) reductase (TIGR02053; EC 1.16.1.1; HMM-score: 25.8) ...
3AOP | Genus
Nitrite and sulphite reductase 4Fe-4S domain. A. PF03460 NIR_SIR_ferr. Nitrite/Sulfite reductase ferredoxin-like half domain. ... Sulfite Reductase Hemoprotein;Domain 2. 3aopA02. 4S39A 3MM5B 2AOPA 3B0HA 3B0NA 3GEOA 3VLXA 3VKPA 4S3DA 3MM7A 4G9PA 3VKTA 4HTRA ... Sulfite Reductase Hemoprotein; domain 1. Sulfite Reductase Hemoprotein, domain 1. 3aopA03. 3.90.480.10. Alpha Beta. Alpha-Beta ... Sulfite Reductase Hemoprotein; domain 1. Sulfite Reductase Hemoprotein, domain 1. 3aopA01. 3.30.413.10. Alpha Beta. 2-Layer ...
RANIERI, Antonio
Unexpected dependence on pH of NO release from Paracoccus pantotrophus cytochrome cd1. - Oxford Neuroscience
The c-heme rapidly oxidised and nitrite was reduced to NO at the d(1)-heme. A slower equilibration of electrons followed, ... A previous study of nitrite reduction by Paracoccus pantotrophus cytochrome cd(1) at pH 7.0 identified early reaction ... Cytochromes, Hydrogen-Ion Concentration, Kinetics, Nitric Oxide, Nitrite Reductases, Nitrites, Oxidation-Reduction, Paracoccus ... The c-heme rapidly oxidised and nitrite was reduced to NO at the d(1)-heme. A slower equilibration of electrons followed, ...
SACOL RS12105 - AureoWiki
Metabolism Energy metabolism Electron transport cytochrome c nitrite reductase, Fe-S protein (TIGR03149; EC 1.7.2.2; HMM-score ... Metabolism Energy metabolism Aerobic periplasmic nitrate reductase, large subunit (TIGR01706; EC 1.7.99.4; HMM-score: 289.5) ... Metabolism Energy metabolism Electron transport periplasmic nitrate reductase, large subunit (TIGR01706; EC 1.7.99.4; HMM-score ... anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family (TIGR02166; HMM-score: 168.7) ...
Phytopathology October 2008 - Volume 98, Number 10
MMTB
NH3 + NADP+ + H2O <=> nitrite + NADPH + H+ 1.7.1.4 nitrite reductase [NAD(P)H] 1.7.7.1 ferredoxin---nitrite reductase 1.8.1.2 ... 1.7.1.10 hydroxylamine reductase (NADH) 1.7.1.15 nitrite reductase (NADH) 1.7.1.4 nitrite reductase [NAD(P)H] - - - ... 1.7.1.10 hydroxylamine reductase (NADH) 1.7.1.4 nitrite reductase [NAD(P)H] 1.7.99.1 hydroxylamine reductase - - - ... nitrite + H2O + NADP+ <=> H+ + nitrate + NADPH 1.7.1.1 nitrate reductase (NADH) 1.7.1.2 nitrate reductase [NAD(P)H] 1.7.1.3 ...
nrfC:Quickview - EcoliWiki
Team:NRP-UEA-Norwich/Week2 - 2012.igem.org
Diamond Publications - Search Results
MSCOVID19: assessing and managing relapses remotely - The MS-Blog
... the enzyme that converts nitrates to nitrite, so your urine, even if you have a UTI, maybe negative for nitrites, however, it ... Please be aware that about a third of UTIs are caused by bacteria that dont produce nitrate reductase, ... Please be aware in the context of a UTI the dipsticks assess two main things; (1) urine nitrite levels and (2) the presence of ... However, positive protein and red blood cells in the absence of the white cells and nitrites are not indicative of a UTI and ...
Ferredoxin-nitrite rPseudomonasEnzymeAmmoniaDenitrificationReductionNADHEscherichiaGeneCytochrome c nitriteNitric oxide reductasesEnzymesSubunitNirSSpinachCatalytic mechanismProteinDenitrifying bacteriaOxidoreductaseGenesElectronAnaerobicCopperNitrogenNrfADenitrificansSubstrateBacterialHydroxylamineMutationHemoproteinNirBCrystallographyRice seedlingsNitrate reductasesOxidase
Ferredoxin-nitrite r6
- In enzymology, a ferredoxin-nitrite reductase (EC 1.7.7.1) is an enzyme that catalyzes the chemical reaction NH3 + 2 H2O + 6 oxidized ferredoxin ⇌ {\displaystyle \rightleftharpoons } nitrite + 6 reduced ferredoxin + 7 H+ The 3 substrates of this enzyme are NH3, H2O, and oxidized ferredoxin, whereas its 3 products are nitrite, reduced ferredoxin, and H+. (wikipedia.org)
- Below are the list of possible Ferredoxin--nitrite reductase products. (mybiosource.com)
- Ferredoxin-Nitrite Reductase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (sickkids.ca)
- This graph shows the total number of publications written about "Ferredoxin-Nitrite Reductase" by people in this website by year, and whether "Ferredoxin-Nitrite Reductase" was a major or minor topic of these publications. (sickkids.ca)
- Below are the most recent publications written about "Ferredoxin-Nitrite Reductase" by people in Profiles. (sickkids.ca)
- Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism. (duke.edu)
Pseudomonas6
- Cyanide binding to fully reduced Pseudomonas aeruginosa cd(1) nitrite reductase (Pa cd(1) NiR) has been investigated for the wild-type enzyme and a site-directed mutant in which the active-site His369 was replaced by Ala. This mutation reduces the affinity toward cyanide (by approximately 13-fold) and especially decreases the rate of binding of cyanide to the reduced d(1) heme (by approximately 100-fold). (rcsb.org)
- After shifting an oxygen-respiring culture of Pseudomonas stutzeri to nitrate or nitrite respiration, we directly monitored the expression of the nirS gene by mRNA analysis. (asm.org)
- The expression of denitrification in the strict sense is sequential in Pseudomonas stutzeri with respect to nitrate respiration, since activation of the narGHJI operon occurs at a higher partial oxygen pressure than that at which the other reductase genes are activated ( 24 , 25 ). (asm.org)
- The periplasmic cytochrome cd 1 nitrite reductase NirS occurring in denitrifying bacteria such as the human pathogen Pseudomonas aeruginosa contains the essential tetrapyrrole cofactors haem c and haem d 1 . (portlandpress.com)
- In the present paper, we summarize the current understanding of the reaction of nitrite reduction in the light of the most recent results on the enzyme from Pseudomonas aeruginosa and discuss the differences between enzymes from different organisms. (biochemsoctrans.org)
- Wharton, DC & Weintraub, ST 1980, ' Identification of nitric oxide and nitrous oxide as products of nitrite reduction by Pseudomonas cytochrome oxidase (nitrite reductase) ', Topics in Catalysis , vol. 97, no. 1, pp. 236-242. (uthscsa.edu)
Enzyme24
- In enzymology, a nitrite reductase (NO-forming) (EC 1.7.2.1) is an enzyme that catalyzes the chemical reaction nitric oxide + H2O + ferricytochrome c ⇌ nitrite + ferrocytochrome c + 2 H+ The 3 substrates of this enzyme are nitric oxide, H2O, and ferricytochrome c, whereas its 3 products are nitrite, ferrocytochrome c, and H+. (wikipedia.org)
- Lastly, since nrfA operon expression is only induced under low-nitrate concentrations, the NrfA enzyme is predicted to have a physiological role only where nitrate (or nitrite) is limiting in the cell environment. (asm.org)
- The NirB nitrite reductase is a soluble siroheme-containing enzyme that uses NADH as an electron donor to reduce nitrite in the cytoplasm. (asm.org)
- The NrfA nitrite reductase is a membrane-associated respiratory enzyme that couples to the membrane-associated formate-oxidizing enzymes via quinones in order to generate membrane potential. (asm.org)
- The abundance of each enzyme is elevated during anaerobic cell growth conditions when either nitrate and/or nitrite is present ( 14 ). (asm.org)
- Nitrite, the substrate for each enzyme, was shown to be a less potent regulatory signal for either operon relative to nitrate in contrast to prior reports. (asm.org)
- This enzyme catalyzes the six-electron reduction of nitrite (NO 2 − ) to ammonia (NH 4 + ) ( 1 ) and its existence has been demonstrated in bacterial strains from almost every taxonomic branch. (pubmedcentralcanada.ca)
- Both membrane nitrate reductase and nitrite reductase enzyme complexes were important for cytotoxicity during the interaction of P. aeruginosa PA14 with THP-1 cells. (asm.org)
- Significant, well defined structural rearrangements in the active site are evident in the series as the enzyme moves through its catalytic cycle, namely nitrite reduction, which is a vital step in the global denitrification process. (rcsb.org)
- The catalytic and spectral properties of the His-tagged, recombinant enzyme are similar, but not identical, to those previously observed for nitrite reductase isolated directly from spinach leaf. (elsevier.com)
- A detailed comparison of the spectral, catalytic and fluorescence properties of nitrite reductase variants, in which each of the enzyme's eight tryptophan residues has been replaced using site-directed mutagenesis by either aromatic or non-aromatic amino acids, has been used to examine possible roles for tryptophan residues in the reduction of nitrite to ammonia catalyzed by the enzyme. (elsevier.com)
- Hydroxylamine oxidoreductase (HAO), the AOB enzyme that catalyzes the 4-electron oxidation of hydroxylamine to nitrite, displays some structural commonalities towards the enzyme cytochrome nitrite reductase (ccNiR, also known as NrfA), which catalyzes the 6-electron reduced amount of nitrite to ammonia in ammonifying bacterias [3C10]. (neurokinin-receptor.info)
- Nitrite reductase is an enzyme operating in the denitrification pathway which catalyses the conversion of nitrite (NO2(-)) to gaseous nitric oxide (NO). Here, crystal structures of the oxidized and reduced forms of the copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3 are presented at 1.74 and 1.85 A resolution, respectively. (chalmers.se)
- Whereas the structure of the enzyme is very similar to those of other copper-containing nitrite reductases, folding as a trimer and containing two copper sites per monomer, the structures reported here enable conformational differences between the oxidized and reduced forms of the enzyme to be identified. (chalmers.se)
- Two sets of PCR primers have been designed to amplify fragments of the gene coding for nitric reductase, a key enzyme involved in bacterial denitrification. (readabstracts.com)
- The enzyme also catalyzed the reduction of NO to N 2 O. No N 2 was identified as a consequence of either nitrite or NO reduction. (uthscsa.edu)
- EPR spectroscopic and chemical analyses of spinach nitrite reductase show that the enzyme contains one reducible iron-sulfur center, and one site for binding either cyanide or nitrite, per siroheme. (duke.edu)
- Complexation of the enzyme with CO (a known ligand for nitrite reductase heme) markedly increases the reducibility of the iron-sulfur center. (duke.edu)
- The EPR spectrum of reduced nitrite reductase in 80% dimethyl sulfoxide establishes clearly that the enzyme contains a tetranuclear iron-sulfur (Fe4S4) center. (duke.edu)
- This novel enzyme indicates (i) separate evolution of nitrite oxidation in " Ca . Nitrotoga" and other NOB, (ii) the possible existence of phylogenetically diverse, unrecognized NOB, and (iii) together with new metagenomic data, the potential existence of nitrite-oxidizing archaea. (asm.org)
- This multiple heme-containing enzyme can reduce nitrite to ammonia. (jcvi.org)
- 5.4 Test Method D7781 uses a nitrate reductase enzyme for the reduction of nitrate to nitrite. (astm.org)
- We are also extending the target of our structural investigation to include the enzyme that prepares the siroheme for incorporation into sulfite reductase hemoprotein. (scripps.edu)
- This enzyme, siroheme synthase, is required for expression of active sulfite reductase. (scripps.edu)
Ammonia13
- The cytochrome c nitrite reductase (ccNiR) from Desulfovibrio desulfuricans ATCC 27774 is able to reduce nitrite to ammonia in a six-electron transfer reaction. (pubmedcentralcanada.ca)
- Cytochrome c nitrite reductase (ccNiR) is involved in the pathway called dissimilatory nitrate reduction to ammonia, thereby playing an important part in the biogeochemical nitrogen cycle. (pubmedcentralcanada.ca)
- Ammonia oxidizers are a widespread and ecologically important group of bacteria that catalyze the oxidation of ammonia to nitrite (NO 2 − ) via hydroxylamine (NH 2 OH) in terrestrial, aquatic, and marine environments ( 5 ). (asm.org)
- It catalyzes the six-electron oxidation of AMMONIA to nitrite. (sickkids.ca)
- Interest in these intermediates is prompted by the presence of iron Cs or iBCs in enzymes that catalyze the reductions of nitrite to ammonia or nitric oxide (nitrite reductases) and the recent identification of cobalt iBC in sulfite reductases, enzymes which are also capable of nitrite reduction. (elsevier.com)
- nitrite reductase, NrfA, Laue crystallography, UV/Vis spectropotentiometry, Proteins film voltammetry Launch Ammonia-nitrite interconversion, a significant area of the natural nitrogen cycle, is certainly completed by a number of bacterias within their respiratory procedure. (neurokinin-receptor.info)
- In one path the ammonia oxidizing bacterias (AOB) such as for example make use of ammonia as an electron donor in respiration, and oxidize it to nitrite [1]. (neurokinin-receptor.info)
- A different course of bacterias uses nitrite being a terminal electron acceptor in the lack of air, reducing it to ammonia in an activity referred to as nitrite ammonification [2]. (neurokinin-receptor.info)
- CcNiR catalyzes the six-electron reduction of nitrite 870823-12-4 to ammonia (Plan 1, Eq. 1), as well as the five-electron reduction of nitric oxide (Plan 1, Eq. 2) and the two-electron reduction of hydroxylamine (Plan 1, Eq. 3) to ammonia [11, 14]. (neurokinin-receptor.info)
- Dissimilatory nitrate reduction to ammonia (DNRA) is the process in which nitrate is reduced, via nitrite, to ammonia. (warwick.ac.uk)
- Polysulphide reductase, NrfD RN [1] RM PMID: 8057835 RT A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria. (jcvi.org)
- We used multiwavelength anomalous diffraction of the native siroheme and Fe 4 S 4 cluster cofactors to solve the atomic resolution structure of sulfite reductase hemoprotein, which catalyzes the concerted 6-electron reductions of sulfite to sulfide and nitrite to ammonia. (scripps.edu)
- Sulfite reductase catalyzes the concerted 6-electron reductions of sulfite to sulfide and nitrite to ammonia. (scripps.edu)
Denitrification9
- nirS encodes the 62-kDa subunit of the homodimeric cytochrome cd 1 nitrite reductase involved in denitrification. (asm.org)
- Our results suggest that a nitrate- and nitrite-responsive regulatory circuit independent of NarXL is necessary for the activation of denitrification genes. (asm.org)
- In the present study, we investigated the signal and regulator requirements for the transcriptional activation of nirS , norCB , and nosZ (i.e., the structural genes for the three reductases involved in nitrite denitrification) following a shifting of the respiratory metabolism from oxygen to nitrate or nitrite. (asm.org)
- By studying narX and narL deletion mutants, we obtained evidence for the existence of a second nitrate- and nitrite-responsive regulatory system in P. stutzeri that is specific for denitrification. (asm.org)
- The cytochrome cd 1 nitrite reductases are enzymes that catalyse the reduction of nitrite to nitric oxide (NO) in the bacterial energy conversion denitrification process. (biochemsoctrans.org)
- Strains lacking genes required for a functional nitrate reductase had decreased fitness as both metals interacted with heme-containing enzymes required for the later steps in the denitrification pathway after nitrate is reduced to nitrite. (frontiersin.org)
- The association with plants affects expression of denitrification genes, the regulation of nitrite and nitric oxide reductases was investigated in Agrobacterium tumefaciens. (readabstracts.com)
- It reduces nitrite to nitric oxide, the first step in denitrification. (nih.gov)
- The goal of this project is to compare the distribution, diversity, and expression of denitrification genes (nitrite reductase) from microorganisms in the two lobes in an attempt to explain this mystery. (nsf.gov)
Reduction18
- Test Methods D3867 uses cadmium for the reduction of nitrate to nitrite. (astm.org)
- The inter- and intra-electron and proton transfers in the nitrite reduction of copper-containing nitrite reductase (CuNiR) were investigated by using the QM/MM method with the calculational models containing type 1 (T1) and type 2 (T2) Cu sites. (rsc.org)
- The electron transfer from the outer electron donor protein to the T1 Cu site occurred both before and after nitrite binding, and nitrite binding lowered the reduction potential of the Cu T1 site. (rsc.org)
- The protonation of catalytic His244 subsequent to nitrite binding and T1 Cu reduction induced partial intra-electron transfer from T1 to T2 Cu sites. (rsc.org)
- Nitrite, the substrate for the two enzymes, must either be encountered environmentally or generated by the cell from nitrate reduction by one of the three E. coli nitrate reductases. (asm.org)
- Solution assays have proved that the specific activity of ccNiR decreases with the reduction potential of the electronic carriers and ammonium is always the main product of nitrite reduction. (pubmedcentralcanada.ca)
- One axial position of the iron atom is occupied by a histidine and the second one is the place of the nitrite reduction. (fu-berlin.de)
- The nirK gene of Rhizobium hedysari HCNT1 encodes nitrite reductase, and the reduction of nitrite causes the production of large concentrations of freely diffusible nitric oxide (NO). The nitrite reductase is structurally similar to the copper containing family of nitrite reductases. (readabstracts.com)
- The bacteria is unable to link nitrite reduction to energy conservation, and the amount of NO it produces is much higher than that produced by other denitrifiers. (readabstracts.com)
- Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase? (expasy.org)
- This serial crystallography approach revealed the gradual conversion of the substrate bound at the catalytic type 2 Cu centre from nitrite to nitric oxide, following reduction of the type 1 Cu electron-transfer centre by X-ray-generated solvated electrons. (rcsb.org)
- These findings shed light on the structural mechanism of the reduction of a copper-bound nitrite to nitric oxide and water. (chalmers.se)
- The reduction of nitrite to NO involves binding of nitrite to the reduced protein at the level of d1-heme, followed by dehydration of nitrite to yield NO and release of the latter. (unicatt.it)
- Pseudoazurin (Paz) is the physiological electron donor to copper-containing nitrite reductase (Nir), which catalyzes the reduction of NO2− to NO. The Nir reaction mechanism involves the reduction of the type 1 (T1) copper electron transfer center by the external physiological electron donor, intramolecular electron transfer from the T1 copper center to the T2 copper center, and nitrite reduction at the type 2 (T2) copper catalytic center. (conicet.gov.ar)
- EPR experiments proved that as a result of the SmPaz/SmNir interaction in the presence of nitrite, the order of the reduction potentials of SmNir reversed, in line with T1 center to T2 center electron transfer being thermodynamically more favorable. (conicet.gov.ar)
- The pentaheme cytochrome c nitrite reductase (NrfA) of Escherichia coli is responsible for nitrite reduction during anaerobic respiration when nitrate is scarce. (uea.ac.uk)
- Both NO and N 2 O were identified by GC/MS as gaseous products of nitrite reduction catalyzed by the cytochrome oxidase (nitrite reductase) purified from Pseudomonasaeruginosa. (uthscsa.edu)
- No N2 was identified as a consequence of either nitrite or NO reduction. (uthscsa.edu)
NADH1
- RT "Location and sequence of the promoter of the gene for the NADH- RT dependent nitrite reductase of Escherichia coli and its regulation by RT oxygen, the Fnr protein and nitrite. (genome.jp)
Escherichia3
- Escherichia coli possesses two distinct nitrite reductase enzymes encoded by the nrfA and nirB operons. (asm.org)
- Escherichia coli possesses two biochemically distinct nitrite reductase enzymes encoded by the nrfABCDEFG and nirBDC operons ( 4 ). (asm.org)
- A system has been developed for expressing a His-tagged form of the ferredoxin-dependent nitrite reductase of spinach in Escherichia coli. (elsevier.com)
Gene14
- Complementary DNA has been isolated that codes for maize nitrite reductase (NiR) by using the corresponding spinach gene (E Back et al . (plantphysiol.org)
- A high percentage of the differences in the DNA sequences is due to the extremely strong bias in the corn gene to have a G/C base in the third codon position with 559/569 codons ending in a G or C. Using a hydroponic system, maize seedlings grown in the absence of an exogenous nitrogen source were induced with nitrate or nitrite. (plantphysiol.org)
- There is also a considerable induction of this gene in roots upon the addition of nitrite, although under the conditions used the final mRNA level was not as high as when nitrate was the inducer. (plantphysiol.org)
- We previously found that the transcript level of the nitrite reductase gene of F. oxysporum , named FoNIIA , was markedly upregulated during conidiation compared with during vegetative growth. (apsnet.org)
- Steady-state gene expression studies revealed a differential pattern of nitrite reductase gene expression where optimal nrfA-lacZ expression occurred only at low to intermediate levels of nitrate and where nirB-lacZ expression was induced only by high nitrate conditions. (asm.org)
- It is unknown how the nrfA and nirB operons are expressed in response to either low or intermediate levels of either nitrate or nitrite since the prior gene regulation studies were performed in batch cultures using high levels of each anion. (asm.org)
- The findings reveal a differential pattern of nitrite reductase gene expression whereby the nrfA operon is preferentially expressed only at low nitrate concentrations. (asm.org)
- Similar mRNA stability and transition kinetics were observed for the norCB operon, encoding the NO reductase complex, and the nosZ gene, encoding nitrous oxide reductase. (asm.org)
- Global gene expression was compared between the Nitrosomonas europaea wild type and a nitrite reductase-deficient mutant using a genomic microarray. (asm.org)
- The gene for a homologue to dissimilatory nitrite reductase, nirK , is present at the end of a four-gene cluster in Nitrosomonas europaea ( 7 ). (asm.org)
- Copper-containing nitrite reductases (CuNiRs), encoded by nirK gene, are found in all kingdoms of life with only 5% of CuNiR denitrifiers having two or more copies of nirK . (sciencemag.org)
- Nitrate, nitrite, nitric oxide and nitrous oxide reducing activities were expressed, and the structural genes for nitrite and nitric oxide reductases were transcribed under anaerobic conditions in the anr mutant strain transformed with the dnr gene. (nih.gov)
- Consensus regions in gene sequences encoding the two forms of nitrite reductase, cd(sub 1)-nir and Cu-nir were used in the preparation of the primers. (readabstracts.com)
- Molecular cloning, characterization, and nucleotide sequence of nit-6, the structural gene for nitrite reductase in Neurospora crassa. (genome.jp)
Cytochrome c nitrite2
- Cytochrome c Nitrite Reductase from Desulfovibrio desulfuricans ATCC 27774: The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA). (expasy.org)
- Members of this protein family are NrfD, a highly hydrophobic protein encoded in the nrf operon, which encodes cytochrome c nitrite reductase. (jcvi.org)
Nitric oxide reductases2
- Ancestral nitric oxide reductases, as well as cytochrome c oxidases and quinol bo oxidases evolved from the former, are capable of binding and detoxifying nitric oxide to nitrous oxide. (elsevier.com)
- Vázquez-Torres, A & Baumler, AJ 2016, ' Nitrate, nitrite and nitric oxide reductases: From the last universal common ancestor to modern bacterial pathogens ', Current Opinion in Microbiology , vol. 29, 1395, pp. 1-8. (elsevier.com)
Enzymes2
- These results shed light on the mechanistic details of the activity of cd 1 nitrite reductases and on the biological role of the d 1 -haem, whose presence in this class of enzymes has to date been unexplained. (biochemsoctrans.org)
- In aerobic soils, nitrate is the dominant species and it is converted to ammonium by the sequential action of two enzymes, nitrate reductase (NR) and nitrite reductase (NiR) (Dechorgnat et al. (thefreelibrary.com)
Subunit3
- Members belong to a broader PFAM protein family, PF03916, which also contains an NrfD-related subunit of polysulphide reductase. (jcvi.org)
- norC and norB encode the cytochrome-c-containing subunit II and cytochrome b-containing subunit I of nitric-oxide reductase (NO reductase), respectively. (tcdb.org)
- Each NOS subunit is divided into 2 domains joined by a calmodulin-binding hinge region: (1) an oxygenase domain with binding sites for heme, tetrahydrobiopterin, and substrate that forms the catalytic center for production of nitric oxide and (2) a reductase domain with binding sites for NADPH, FAD, and FMN that supplies electrons to the oxygenase domain. (scripps.edu)
NirS5
- The continued transcription of the nirS operon required the presence of nitrate or nitrite. (asm.org)
- By monitoring the production of narH and nirS transcripts of Paracoccus denitrificans , it has been shown that induction of nitrate reductase precedes that of nitrite reductase ( 8 ). (asm.org)
- Furthermore, deletion mutations in genes encoding membrane nitrate reductase (Δ narGH ) and nitrite reductase (Δ nirS ) produced defects in the expression of type III secretion system (T3SS) components, extracellular protease, and elastase. (asm.org)
- Addition of exogenous nitric oxide (NO)-generating compounds to Δ nirS mutant cultures restored the production of T3SS phospholipase ExoU, whereas nitrite addition had no effect. (asm.org)
- These data suggest that NO generated via nitrite reductase NirS contributes to the regulation of expression of selected virulence factors in P. aeruginosa PA14. (asm.org)
Spinach1
- Knaff, David B. / The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach . (elsevier.com)
Catalytic mechanism1
- Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. (ebi.ac.uk)
Protein2
- Nitrite oxidation followed Michaelis-Menten kinetics, with an apparent K m ( K m (app) ) of ~89 µM nitrite and a V max of ~28 µmol of nitrite per mg of protein per h. (asm.org)
- Dr. McCarthy's recent work produced a nitrate reductase mutant strain of P. tricornutum , described how the loss of function affected the morphology and viability of the cell and pointed to physiological and molecular mechanisms that drive vacuolar storage of nitrate and the possibility of nitrate reductase-vacuolar transport protein complexes. (jcvi.org)
Denitrifying bacteria1
- It is unknown which N -oxide-sensitive regulatory system controls the genes encoding the reductases of denitrifying bacteria that act on the substrates nitrite, nitric oxide, and nitrous oxide and to what extent their activation depends on coordinately and/or sequentially acting regulators. (asm.org)
Oxidoreductase1
- Ca . Nitrotoga fabula" possesses a new type of periplasmic nitrite oxidoreductase belonging to a lineage of mostly uncharacterized proteins. (asm.org)
Genes2
- These chlorotic plants strongly resemble those transformed with a 35S-Nii (nitrite reductase) transgene, in which both Nii host genes and the 35S-Nii transgene are silenced by co-suppression. (deepdyve.com)
- reductase) transgene, in which both Nii host genes and the 35S- Nii transgene are silenced by co-suppressi on. (deepdyve.com)
Electron1
- The proton transfer from His244 to nitrite bound on the T2 Cu site via the hydrogen bond network induced intra-electron transfer from the T1 to T2 Cu site. (rsc.org)
Anaerobic4
- The expression of each operon is induced during anaerobic cell growth conditions and is further modulated by the presence of either nitrite or nitrate in the cells' environment. (asm.org)
- To examine how each operon is expressed at low, intermediate, and high levels of either nitrate or nitrite, anaerobic chemostat culture techniques were employed using nrfA-lacZ and nirB-lacZ reporter fusions. (asm.org)
- Thus, we examined the steady-state expression of nrfA-lacZ and nirB-lacZ reporter fusions using anaerobic chemostat culture methods under limiting nitrite or nitrate conditions. (asm.org)
- NO detoxification by NO reductase during anaerobic growth is therefore important for maintenance of cell function. (asm.org)
Copper8
- Molecular characterization of a copper-containing nitrite reductase from Rhodopseudomonas sphaeriodes forma sp. (wikipedia.org)
- Here, we explore this idea in a tethered 3-domain, trimeric copper-containing nitrite reductase. (nih.gov)
- Rationale and strategy for studying the role of redox partner tethering in copper containing nitrite reductase. (nih.gov)
- top) and proposed mechanism (bottom) of the 3-domain copper containing nitrite reductase, Rp NiR, used in this study. (nih.gov)
- Recent structural insights into the function of copper nitrite reductases. (ebi.ac.uk)
- Rapid, shutterless X-ray detector technology on a synchrotron MX beamline was exploited to perform low-dose serial crystallography on a single copper nitrite reductase crystal, which survived long enough for 45 consecutive 100 K X-ray structures to be collected at 1.07-1.62 Å resolution, all sampled from the same crystal volume. (rcsb.org)
- This family consists of copper-type nitrite reductase. (nih.gov)
- Copper-containing nitrite reductase harbors a type-1 and a type-2 Cu site. (forskningsdatabasen.dk)
Nitrogen4
- 1.1 This test method is applicable to the determination of nitrate plus nitrite (as nitrogen) in drinking water, surface, saline, wastewater, and ground waters. (astm.org)
- From the 1940s to the 1970s, several studies indicated that a microbe was missing from nature that could anaerobically oxidize ammonium, with nitrate or nitrite, to dinitrogen gas and that the nitrogen cycle ( Fig. 1 ) thus contained more reactions than was known at that time ( 8 , 29 , 73 ). (asm.org)
- 1.1 These test methods cover the determination of nitrite nitrogen, nitrate nitrogen, and combined nitrite-nitrate nitrogen in water and wastewater in the range from 0.05 to 1.0 mg/L nitrogen. (astm.org)
- Sulfite and nitrite reductases catalyze fundamental chemical transformations for biogeochemical cycling of sulfur and nitrogen. (scripps.edu)
NrfA2
Denitrificans1
- Recently, the structure of a Cu-containing nitrite reductase (NiR) from Hyphomicrobium denitrificans ( Hd NiR) has been reported, establishing the existence of a new family of Cu-NiR where an additional type 1 Cu (T1Cu) containing cupredoxin domain is located at the N-terminus (Nojiri et al. (springer.com)
Substrate2
- We have evidence that release of NO from the ferrous d 1 -haem occurs rapidly enough to be fully compatible with the turnover, in contrast with previous hypotheses, and that the substrate nitrite is able to displace NO from the d 1 -haem iron. (biochemsoctrans.org)
- Nitrite reductase and NO reductase (with succinate or ascorbate as substrates) and nitrous oxide reductase (with succinate as substrate) activities were not detected in these mutant strains. (tcdb.org)
Bacterial3
- The electrochemical gradient that ensues from the enzymatic activity of cytochromes such as nitrate reductase, nitric oxide reductase, and quinol oxidase contributes to the bioenergetics of the bacterial cell. (elsevier.com)
- The finally formed NO (in this particular bacterial nitrite reductase) is replaced by a hydroxo ligand. (fu-berlin.de)
- The heme-containing periplasmic nitrite reductase (cd1 NIR) is responsible for the production of nitric oxide (NO) in denitrifying bacterial species, among which are several animal and plant pathogens. (unicatt.it)
Hydroxylamine1
- In addition to nitrite, some ccNiRs were shown to reduce other substrates like nitric oxide, hydroxylamine, o-methylhydroxylamine [ 6 ], or sulphite [ 7 , 8 ]. (pubmedcentralcanada.ca)
Mutation1
- Mutation of this glutamine to the more usual calcium ligand, glutamate, results in an increase in the Km for nitrite by around 10-fold, while Vmax is unaltered. (uea.ac.uk)
Hemoprotein2
- We determined 12 key high-resolution structures of sulfite reductase hemoprotein that characterize its active center in 3 different states of oxidation and its interactions with substrates, inhibitors, intermediates, and products. (scripps.edu)
- We used multiwavelength anomalous diffraction of the native siroheme, an iron-containing macrocycle of the isobacteriochlorin class, and Fe 4 S 4 cluster cofactors to solve the atomic-resolution structure of the hemoprotein from sulfite reductase hemoprotein. (scripps.edu)
NirB2
Crystallography1
- The high-yield expression and purification of cytochrome nitrite reductase (ccNiR), and its own characterization by a variety of methods, notably Laue crystallography, is reported. (neurokinin-receptor.info)
Rice seedlings2
- Effect of inhibition of the Hill reaction on polyribosomes level and on induced synthesis of nitrate and nitrite reductases in rice seedlings. (bvsalud.org)
- Some properties of nitrate and nitrite reductases from rice seedlings. (bvsalud.org)
Nitrate reductases2
- 2. Nason, A. Nitrate reductases. (qmul.ac.uk)
- 1. Nason, A. Nitrate reductases. (qmul.ac.uk)
Oxidase1
- It transfers electrons between Complexes III (Coenzyme Q - Cyt C reductase) and IV (Cyt C oxidase). (wikipedia.org)