Nitrate Reductase and Nitrite Reductase Activity in Dark-Grown Radish Seedlings: Relation to the Supply of NADPH

1976 ◽  
Vol 37 (2) ◽  
pp. 139-142 ◽  
Author(s):  
INEKE STULEN ◽  
L. LANTING
1989 ◽  
Vol 35 (11) ◽  
pp. 1061-1064 ◽  
Author(s):  
P. Bonin ◽  
M. Gilewicz ◽  
J. C. Bertrand

Studies on the effect of oxygen on denitrification have shown that denitrification on Pseudomonas nautica 617 can take place in the presence of oxygen. The enzymes associated with denitrification are affected differently with respect to oxygen concentration. Nitrate reductase was less sensitive toward oxygen than nitrite and nitrous oxide reductases. Nitrate reductase activity was completely blocked at an oxygen concentration greater than 4.05 mg/L, compared with 2.15 and 0.25 mg/L for nitrite and nitrous oxide reductases, respectively. After an aerobic–anaerobic shift, nitrate reductase activity remained unchanged whereas the rate of nitrite reductase activity rose to a value only 20% that of the original rate.Key words: denitrification, oxygen, Pseudomonas.


1998 ◽  
Vol 180 (20) ◽  
pp. 5344-5350 ◽  
Author(s):  
Michiko M. Nakano ◽  
Tamara Hoffmann ◽  
Yi Zhu ◽  
Dieter Jahn

ABSTRACT The nitrate and nitrite reductases of Bacillus subtilishave two different physiological functions. Under conditions of nitrogen limitation, these enzymes catalyze the reduction of nitrate via nitrite to ammonia for the anabolic incorporation of nitrogen into biomolecules. They also function catabolically in anaerobic respiration, which involves the use of nitrate and nitrite as terminal electron acceptors. Two distinct nitrate reductases, encoded bynarGHI and nasBC, function in anabolic and catabolic nitrogen metabolism, respectively. However, as reported herein, a single NADH-dependent, soluble nitrite reductase encoded by the nasDE genes is required for both catabolic and anabolic processes. The nasDE genes, together with nasBC(encoding assimilatory nitrate reductase) and nasF(required for nitrite reductase siroheme cofactor formation), constitute the nas operon. Data presented show that transcription of nasDEF is driven not only by the previously characterized nas operon promoter but also from an internal promoter residing between the nasC andnasD genes. Transcription from both promoters is activated by nitrogen limitation during aerobic growth by the nitrogen regulator, TnrA. However, under conditions of oxygen limitation,nasDEF expression and nitrite reductase activity were significantly induced. Anaerobic induction of nasDEFrequired the ResDE two-component regulatory system and the presence of nitrite, indicating partial coregulation of NasDEF with the respiratory nitrate reductase NarGHI during nitrate respiration.


1985 ◽  
Vol 12 (6) ◽  
pp. 631 ◽  
Author(s):  
SF Ledgard ◽  
KC Woo ◽  
FJ Bergersen

The isotopic fractionations of nitrogen during the reduction of NO3- and NO2- in a cytosolic fraction and in a chloroplast preparation from spinach (Spinacia oleracea L.) leaves were determined. The reduction of NO3- to NH3 was studied using a reconstituted system containing cytosolic extract and intact chloroplasts, while a chloroplast system was used for NO2- reduction. In the reconstituted systems the ratio of nitrate reductase activity to nitrite reductase activity had a large effect on the relative amounts of NO2- and NH3 formed. Ammonia predominated when the nitrate reductase to nitrite reductase activity ratio was 1 : 5 and this ratio was used in the isotopic fractionation studies. Significant isotopic fractionation of N was observed in the reconstituted system but not in the chloroplast system. This indicates that the observed isotopic fractionation was associated with the reduction of NO3- to NO2- by nitrate reductase. The isotopic fractionation (i.e. δ15Nproduct - δ15Nsubstrate) for this reaction was - 15‰.


1991 ◽  
Vol 37 (10) ◽  
pp. 744-750 ◽  
Author(s):  
Christian Chauret ◽  
Roger Knowles

Tungstate, at concentrations that completely suppressed nitrate reductase activity in Paracoccus denitrificans, caused only partial inhibition of nitrate reductase in Azospirillum brasilense Sp7. Nitrate reductase activity in cell-free extracts was much more sensitive than whole cells to tungstate, suggesting that there may be a barrier to its transport. Nitrite reductase activity was partially inhibited by tungstate in both whole cells and cell-free extracts. Azospirillum brasilense apparently scavenged enough contaminating molybdenum from molybdenum-limited medium to allow maximum nitrate reductase activity, which was not stimulated by added molybdate. Cells grown in molybdenum-depleted medium could not reduce nitrate. Nitrate concentrations less than 0.25 mM inhibited activity, but not synthesis, of nitrite reductase and caused significant accumulation of nitrite during reduction of nitrate. Key words: Azospirillum brasilense, Paracoccus denitrificans, nitrate reductase, nitrite reductase, tungsten, molybdenum, denitrification.


1978 ◽  
Vol 24 (1) ◽  
pp. 45-49 ◽  
Author(s):  
F. Pichinoty ◽  
J.-L. Garcia ◽  
C. Job ◽  
M. Durand

The denitrifying capacity of 15 strains of Bacillus licheniformis was evaluated. In general, N2 production by the cultures on complex media containing NO3− is irregular and quite slow and three of the strains never produce gas. Bacillus licheniformis grows rapidly in anaerobiosis on peptone medium containing NO3− which is reduced to NO2−. None of the strains grow in peptone medium with NO2− or N2O as the respiratory substrate, nor do they grow under an atmosphere of 10% NO–90% N2. Denitrification was studied in cell suspensions using gas chromatography. N2O production from NO3− or NO2− is always weak at best; nitric oxide is reduced to N2O at an appreciable rate. All the strains synthesize nitrate reductase A in anaerobiosis when NO3− is present. In cell extracts, nitrite reductase activity is always negligible or nil with tetramethyl-p-phenylenediamine as an electron donor.


2014 ◽  
Vol 2 (S1) ◽  
Author(s):  
V Simon ◽  
A Dyson ◽  
M Minnion ◽  
M Feelisch ◽  
M Singer

2016 ◽  
Vol 55 (9) ◽  
pp. 4233-4247 ◽  
Author(s):  
Steven M. Berry ◽  
Jacob N. Strange ◽  
Erika L. Bladholm ◽  
Balabhadra Khatiwada ◽  
Christine G. Hedstrom ◽  
...  

2009 ◽  
Vol 296 (2) ◽  
pp. H237-H246 ◽  
Author(s):  
Arlin B. Blood ◽  
Mauro Tiso ◽  
Shilpa T. Verma ◽  
Jennifer Lo ◽  
Mahesh S. Joshi ◽  
...  

Growing evidence indicates that nitrite, NO2−, serves as a circulating reservoir of nitric oxide (NO) bioactivity that is activated during physiological and pathological hypoxia. One of the intravascular mechanisms for nitrite conversion to NO is a chemical nitrite reductase activity of deoxyhemoglobin. The rate of NO production from this reaction is increased when hemoglobin is in the R conformation. Because the mammalian fetus exists in a low-oxygen environment compared with the adult and is exposed to episodes of severe ischemia during the normal birthing process, and because fetal hemoglobin assumes the R conformation more readily than adult hemoglobin, we hypothesized that nitrite reduction to NO may be enhanced in the fetal circulation. We found that the reaction was faster for fetal than maternal hemoglobin or blood and that the reactions were fastest at 50–80% oxygen saturation, consistent with an R-state catalysis that is predominant for fetal hemoglobin. Nitrite concentrations were similar in blood taken from chronically instrumented normoxic ewes and their fetuses but were elevated in response to chronic hypoxia. The findings suggest an augmented nitrite reductase activity of fetal hemoglobin and that the production of nitrite may participate in the regulation of vascular NO homeostasis in the fetus.


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