Reaction Systems Related to Dissimilatory Nitrate Reductase:  Nitrate Reduction Mediated by Bis(dithiolene)tungsten Complexes

2005 ◽  
Vol 44 (4) ◽  
pp. 1068-1072 ◽  
Author(s):  
Jianfeng Jiang ◽  
R. H. Holm
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Reaction Systems ◽  
Tungsten Complexes

Some metabolic responses of bush bean plants to a subherbicidal concentration of certain s-triazine compounds

1970 ◽  
Vol 48 (12) ◽  
pp. 2213-2217 ◽  
Author(s):  
B. Singh ◽  
D. K. Salunkhe
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Adenosine Triphosphatase ◽  
Acid Synthesis ◽  
Controlled Environment ◽  
Transaminase Activity ◽  
Starch Phosphorylase ◽  
Phaseolus Vulgaris L ◽  
Bean Plants ◽  
Bush Bean

A solution containing 0.5 p.p.m. of atrazine, simazine, igran, or GS-14254 with 0.2% triton-B 1956 was applied to the foliage of 11-day-old seedlings of bush beans, Phaseolus vulgaris L. cultivar Tender-green, growing on vermiculite in a controlled environment. The activities of nitrate reductase, glutamic-pyruvic transaminase, α-amylase, starch phosphorylase, and adenosine triphosphatase were determined 5,10, and 20 days after treatment. In general, the activity of each of the five enzymes was stimulated by the treatment. The results suggest that protein increase following the application of.s-triazines to bean plants may stem in part from an enhanced rate of amino acid formation resulting from the induced increment in nitrate reductase and transaminase activity. The application of these chemicals also creates a metabolic condition favorable for greater use of carbohydrates needed for nitrate reduction and protein synthesis, and as a source of organic acid synthesis.

Molybdenum incorporation in denitrifying Azospirillum brasilense Sp7

1992 ◽  
Vol 38 (10) ◽  
pp. 1042-1047 ◽  
Author(s):  
Christian Chauret ◽  
Wilfredo L. Barraquio ◽  
Roger Knowles
Keyword(s):  
Nitrate Reductase ◽  
Key Words ◽  
Nitrate Reduction ◽  
Gel Electrophoresis ◽  
Azospirillum Brasilense ◽  
Paracoccus Denitrificans ◽  
Free Medium ◽  
Azospirillum Brasilense Sp7

Nondenaturating disc gel electrophoresis revealed that 99Mo was incorporated into the nitrate reductase of Azospirillum brasilense grown in the absence but not in the presence of tungstate. Under denitrifying conditions, A. brasilense grown in tungsten-free medium steadily accumulated 99Mo for 12 h. In contrast, Paracoccus denitrificans grown under the same conditions ceased uptake after 1 h. However, both bacteria were incapable of accumulating significant amounts of 99Mo in media containing 10 mM tungstate, even though nitrate was reduced by A. brasilense. Aerobically grown A. brasilense cells transported 99Mo more efficiently than anaerobically grown cells. Key words: Azospirillum brasilense, tungsten, molybdenum incorporation, nitrate reduction.

Voltammetric characterization of the aerobic energy-dissipating nitrate reductase of Paracoccus pantotrophus: exploring the activity of a redox-balancing enzyme as a function of electrochemical potential

2007 ◽  
Vol 409 (1) ◽  
pp. 159-168 ◽  
Author(s):  
Andrew J. Gates ◽  
David J. Richardson ◽  
Julea N. Butt
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Reductase Activity ◽  
Electrochemical Potential ◽  
Intact Cells ◽  
Protein Film ◽  
Protein Film Voltammetry ◽  
Voltammetric Studies ◽  
Paracoccus Pantotrophus

Paracoccus pantotrophus expresses two nitrate reductases associated with respiratory electron transport, termed NapABC and NarGHI. Both enzymes derive electrons from ubiquinol to reduce nitrate to nitrite. However, while NarGHI harnesses the energy of the quinol/nitrate couple to generate a transmembrane proton gradient, NapABC dissipates the energy associated with these reducing equivalents. In the present paper we explore the nitrate reductase activity of purified NapAB as a function of electrochemical potential, substrate concentration and pH using protein film voltammetry. Nitrate reduction by NapAB is shown to occur at potentials below approx. 0.1 V at pH 7. These are lower potentials than required for NarGH nitrate reduction. The potentials required for Nap nitrate reduction are also likely to require ubiquinol/ubiquinone ratios higher than are needed to activate the H+-pumping oxidases expressed during aerobic growth where Nap levels are maximal. Thus the operational potentials of P. pantotrophus NapAB are consistent with a productive role in redox balancing. A Michaelis constant (KM) of approx. 45 μM was determined for NapAB nitrate reduction at pH 7. This is in line with studies on intact cells where nitrate reduction by Nap was described by a Monod constant (KS) of less than 15 μM. The voltammetric studies also disclosed maximal NapAB activity in a narrow window of potential. This behaviour is resistant to change of pH, nitrate concentration and inhibitor concentration and its possible mechanistic origins are discussed.

scholarly journals Activity of Spore-Specific Respiratory Nitrate Reductase 1 ofStreptomyces coelicolorA3(2) Requires a Functional Cytochromebcc-aa3Oxidase Supercomplex

2019 ◽  
Vol 201 (11) ◽  
Author(s):  
Dörte Falke ◽  
Bianca Biefel ◽  
Alexander Haase ◽  
Stefan Franke ◽  
Marco Fischer ◽  
...  
Keyword(s):  
Membrane Potential ◽  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Streptomyces Coelicolor ◽  
Nitrate Respiration ◽  
Nitrate Transport ◽  
Developmental Cycle ◽  
Content Type ◽  
Resting Spores ◽  
Respiratory Nitrate Reductase

ABSTRACTSpores have strongly reduced metabolic activity and are produced during the complex developmental cycle of the actinobacteriumStreptomyces coelicolor. Resting spores can remain viable for decades, yet little is known about how they conserve energy. It is known, however, that they can reduce either oxygen or nitrate using endogenous electron sources.S. coelicoloruses either a cytochromebdoxidase or a cytochromebcc-aa3oxidase supercomplex to reduce oxygen, while nitrate is reduced by Nar-type nitrate reductases, which typically oxidize quinol directly. Here, we show that in resting spores the Nar1 nitrate reductase requires a functionalbcc-aa3supercomplex to reduce nitrate. Mutants lacking the completeqcr-ctagenetic locus encoding thebcc-aa3supercomplex showed no Nar1-dependent nitrate reduction. Recovery of Nar1 activity was achieved by genetic complementation but only when the completeqcr-ctalocus was reintroduced to the mutant strain. We could exclude that the dependence on the supercomplex for nitrate reduction was via regulation of nitrate transport. Moreover, the catalytic subunit, NarG1, of Nar1 was synthesized in theqcr-ctamutant, ruling out transcriptional control. Constitutive synthesis of Nar1 in mycelium revealed that the enzyme was poorly active in this compartment, suggesting that the Nar1 enzyme cannot act as a typical quinol oxidase. Notably, nitrate reduction by the Nar2 enzyme, which is active in growing mycelium, was not wholly dependent on thebcc-aa3supercomplex for activity. Together, our data suggest that Nar1 functions together with the proton-translocatingbcc-aa3supercomplex to increase the efficiency of energy conservation in resting spores.IMPORTANCEStreptomyces coelicolorforms spores that respire with either oxygen or nitrate, using only endogenous electron donors. This helps maintain a membrane potential and, thus, viability. Respiratory nitrate reductase (Nar) usually receives electrons directly from reduced quinone species; however, we show that nitrate respiration in spores requires a respiratory supercomplex comprising cytochromebccoxidoreductase andaa3oxidase. Our findings suggest that the Nar1 enzyme in theS. coelicolorspore functions together with the proton-translocatingbcc-aa3supercomplex to help maintain the membrane potential more efficiently. Dissecting the mechanisms underlying this survival strategy is important for our general understanding of bacterial persistence during infection processes and of how bacteria might deal with nutrient limitation in the natural environment.

Electron Transport to Assimilatory Nitrate Reductase in A zotobacter vinelandii

1981 ◽  
Vol 36 (11-12) ◽  
pp. 1030-1035 ◽  
Author(s):  
Hermann Bothe ◽  
Klaus-Peter Häger
Keyword(s):  
Electron Transport ◽  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Azotobacter Vinelandii ◽  
Additive Effects ◽  
Electron Carrier ◽  
Transport Chain ◽  
Solubilized Enzyme ◽  
Electron Carriers ◽  
Bound Electron

Abstract Assimilatory nitrate reductase was particle-bound in extracts from Azotobacter vinelandii. Nitrate reduction by particle fractions was dependent on NADPH and a particle-bound electron carrier. When the enzyme was solubilized from the particles by treatment with detergents, the particle-bound electron carrier could be substituted by ferredoxin or flavodoxin. Flavodoxin reduced at the expense of photoreduced deazaflavin was much more efficient than ferredoxin in transferring electrons to nitrate reductase. The addition of both ferredoxin and flavodoxin to the assays with photoreduced deazaflavin gave additive effects. With the solubilized enzyme, NADPH only poorly supported nitrate reduction even after the addition of electron carriers. The experiments indicate that A. vinelandii utilizes an electron transport chain between NADPH and nitrate reductase with some properties similar to those described for the generation of reductants to nitrogenase.

scholarly journals Novel growth characteristics and high rates of nitrate reduction of anEscherichia colistrain, LCB2048, that expresses only a periplasmic nitrate reductase

2000 ◽  
Vol 185 (1) ◽  
pp. 51-57 ◽  
Author(s):  
Laura C. Potter ◽  
Paul D. Millington ◽  
Gavin H. Thomas ◽  
Richard A. Rothery ◽  
Gérard Giordano ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Growth Characteristics ◽  
Periplasmic Nitrate Reductase

scholarly journals Contribution of shoots and roots to in vivo nitrate reduction in NADH-specific nitrate reductase-deficient mutant seedlings of barley (Hordeum vulgareL.)

2004 ◽  
Vol 50 (4) ◽  
pp. 527-535 ◽  
Author(s):  
Salwa Abdel-Latif ◽  
Tahei Kawachi ◽  
Hiroyuki Fujikake ◽  
Norikuni Ohtake ◽  
Takuji Ohyama ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Deficient Mutant
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