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1.
Braz J Biol ; 83: e264218, 2023.
Article in English | MEDLINE | ID: mdl-37194794

ABSTRACT

In a vegetation experiment with soybean plants of the Svapa and Mageva varieties and in a field experiment with bean plants of the Geliada and Shokoladnitsa varieties, we studied the effect of pre-sowing treatment of the seeds of these plants with Rizotorfin and Epin-extra on the nitrogenase activity of the nodules of these plants and their ultrastructure. Analysis of the ultrastructure of the nodule tissue of beans and soybeans was carried out in the flowering phase. It was found that the highest indices of the mass and number of nodules and the activity of nitrogenase in them were found in bean plants of the Heliada cultivar when the seeds were treated with Epin-extra against the background of inoculation with Rizotorfin, where the largest area of symbiosomes, volutin and their number was noted in the nodules. Beans of the Shokoladnitsa variety showed the protective effect of Rizotorfin. In the nodules of soybean plants of the Svapa variety, the seeds of which were treated with Epin-extra against the background of inoculation with Rizotorfin, the presence of a large number of symbiosomes, bacteroids, volutin inclusions with a larger area and a minimum number of inclusions of poly-ß-hydroxybutyric acid (PHB) was noted, and the highest indicators of symbiotic activity. Soybean plants of the Mageva variety showed the protective effect of Rizotorfin. The efficiency of the symbiotic system was determined by the number and weight of nodules and the activity of the nitrogenase enzyme.


Subject(s)
Fabaceae , Glycine max , Nitrogenase/metabolism , Nitrogenase/pharmacology , Vegetables , Symbiosis , Nitrogen Fixation
2.
J Environ Qual ; 33(3): 825-31, 2004.
Article in English | MEDLINE | ID: mdl-15224916

ABSTRACT

Glyphosate-resistant (GR) soybean [Glycine max (L.) Merr.] expressing an insensitive 5-enolpyruvylshikimic acid-3-phosphate synthase (EPSPS) gene has revolutionized weed control in soybean production. The soybean nitrogen fixing symbiont, Bradyrhizobium japonicum, possesses a glyphosate-sensitive enzyme and upon exposure to glyphosate accumulates shikimic acid and hydroxybenzoic acids such as protocatechuic acid (PCA), accompanied with B. japonicum growth inhibition and death at high concentrations. In a series of greenhouse and field experiments, glyphosate inhibited nodulation and nodule leghemoglobin content of GR soybean. Glyphosate accumulated in nodules of field-grown GR soybean, but its effect on nitrogenase activity of GR soybean was inconsistent in field studies. In greenhouse studies, nitrogenase activity of GR soybean following glyphosate application was transiently inhibited especially in early growth stages, with the greatest inhibition occurring under moisture stress. Studies using bacteroid preparations showed that the level of glyphosate inhibition of bacteroid nitrogenase activity was related to in vitro glyphosate sensitivity of the B. japonicum strains. These studies indicate the potential for reduced nitrogen fixation in the GR soybean system; however, yield reductions due to this reduced N2 fixation in early stages of growth have not been demonstrated.


Subject(s)
Bradyrhizobium/physiology , Glycine max/genetics , Glycine/analogs & derivatives , Glycine/pharmacology , Herbicides/pharmacology , Plants, Genetically Modified , Symbiosis , Insecticide Resistance/genetics , Nitrogen/metabolism , Nitrogenase/pharmacology , Plant Roots/microbiology , Glycine max/enzymology , Water , Glyphosate
3.
Chemosphere ; 50(8): 1055-61, 2003 Mar.
Article in English | MEDLINE | ID: mdl-12531712

ABSTRACT

Klebsiella oxytoca, isolated from cyanide-containing industrial wastewater, was shown to be able to biodegrade cyanide to non-toxic endproducts using cyanide as the sole nitrogen source. In this study, ammonia was one of the detected endproduct of cyanide biodegradation by the concentrated resting cells of K. oxytoca. Moreover, cyanide has been shown to be biotransformed to methane through the actions of concentrated resting cells. Biodegradation of cyanide by cell-free extracts was not observed, which might be due to the inactivation of nitrogenase (an oxygen-labial enzyme) caused by the oxygen exposure after cell disruption. Results show that the cyanide consumption by resting cells of K. oxytoca was induced when the pretreatment of these cells with cyanide was conducted. However, the cyanide-degrading capability of resting cells pretreated with ammonia was inhibited. The inhibition of cyanide degradation by resting cells of K. oxytoca was affected by the ammonia concentration. This might result from the suppression of nitrogenase activity of K. oxytoca by ammonia since nitrogenase was suggested to be the sole cyanide-degrading enzyme during the cyanide degradation process. Results from this study also show that the processes of cyanide biodegradation and ammonia production by resting cells occurred simultaneously. This suggests that the utilization of cyanide as nitrogen source by K. oxytoca might proceed using ammonia as an assimilatory substrate.


Subject(s)
Ammonia/chemistry , Hydrogen Cyanide/metabolism , Klebsiella oxytoca/physiology , Methane/chemistry , Water Pollutants, Chemical/metabolism , Water Purification/methods , Biotransformation , Industrial Waste , Nitrogenase/pharmacology
4.
J Environ Biol ; 22(2): 79-81, 2001 Apr.
Article in English | MEDLINE | ID: mdl-11500021

ABSTRACT

In an experiment, application of different levels of metalaxyl to a sandy loam soil significantly affected the nodulation and nitrogenase activity of mungbean. In both the compost amended and unamended soils, 0.5 mg kg(-1) of metalaxyl enhanced acetylene reduction activity and yield of mungbean, where as higher concentrations (1 mg and 2.5 mg kg(-1) of fungicide) inhibited the nodulation traits as well as economic traits of mungbean.


Subject(s)
Acetylene/metabolism , Alanine/analogs & derivatives , Alanine/adverse effects , Fabaceae/enzymology , Fungicides, Industrial/adverse effects , Nitrogenase/drug effects , Bradyrhizobium , Fabaceae/drug effects , Fabaceae/growth & development , Nitrogenase/pharmacology , Plant Roots/microbiology
5.
J Inorg Biochem ; 80(1-2): 133-6, 2000 May 30.
Article in English | MEDLINE | ID: mdl-10885473

ABSTRACT

The topic, vanadium nitrogenase, is reviewed with respect to biological characteristics and findings on its structure and functions. Structural models (vanadium complexes containing ligands related to the active center in the iron-vanadium cofactor) and functional models for the reductive protonation of dinitrogen, the activation of alkynes and reductive C-C coupling of isocyanides are addressed.


Subject(s)
Nitrogenase , Binding Sites , Models, Molecular , Molecular Structure , Nitrogenase/chemistry , Nitrogenase/pharmacology
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