Noncoupled NADH:ubiquinone oxidoreductase of Azotobacter vinelandii is required for diazotrophic growth at high oxygen concentrations.
نویسندگان
چکیده
The gene encoding the noncoupled NADH:ubiquinone oxidoreductase (NDH II) from Azotobacter vinelandii was cloned, sequenced, and used to construct an NDH II-deficient mutant strain. Compared to the wild type, this strain showed a marked decrease in respiratory activity. It was unable to grow diazotrophically at high aeration, while it was fully capable of growth at low aeration or in the presence of NH(4)(+). This result suggests that the role of NDH II is as a vital component of the respiratory protection mechanism of the nitrogenase complex in A. vinelandii. It was also found that the oxidation of NADPH in the A. vinelandii respiratory chain is catalyzed solely by NDH II.
منابع مشابه
Coordinated expression of fdxD and molybdenum nitrogenase genes promotes nitrogen fixation by Rhodobacter capsulatus in the presence of oxygen.
Rhodobacter capsulatus is able to grow with N2 as the sole nitrogen source using either a molybdenum-dependent or a molybdenum-free iron-only nitrogenase whose expression is strictly inhibited by ammonium. Disruption of the fdxD gene, which is located directly upstream of the Mo-nitrogenase genes, nifHDK, abolished diazotrophic growth via Mo-nitrogenase at oxygen concentrations still tolerated ...
متن کاملCytochrome and ubiquinone patterns during growth of Azotobacter vinelandii.
After synthesis during the early log phase, the concentrations of ubiquinone and cytochromes did not vary during the growth cycle of Azotobacter vinelandii, when grown with either high or low aeration on nitrogen-free or urea-containing media. The level of aeration had no effect on the concentrations of the electron carriers synthesized, but affected the growth rate. On urea-containing medium, ...
متن کاملThe genes encoding the delta subunits of dinitrogenases 2 and 3 are required for mo-independent diazotrophic growth by Azotobacter vinelandii.
vnfG and anfG encode the delta subunits of alternative nitrogenases 2 and 3 in Azotobacter vinelandii, respectively. As a first step towards elucidating the role of these subunits, diazotrophic growth and acetylene reduction studies were conducted on mutants containing alterations in the genes encoding these subunits. Mutants containing a stop codon (C36stop) or an in-frame deletion in anfG wer...
متن کاملMutational inactivation of a gene homologous to Escherichia coli ptsP affects poly-beta-hydroxybutyrate accumulation and nitrogen fixation in Azotobacter vinelandii.
Strain DS988, an Azotobacter vinelandii mutant with a reduced capacity to accumulate poly-beta-hydroxybutyrate, was isolated after mini-Tn5 mutagenesis of the UW136 strain. Cloning and nucleotide sequencing of the affected locus revealed a gene homologous to Escherichia coli ptsP which encodes enzyme INtr, a homologue of enzyme I of the phosphoenol pyruvate-sugar phosphotransferase system with ...
متن کاملNature of oxygen inhibition of nitrogenase from Azotobacter vinelandii.
The reduction of nitrogen, acetylene, azide, and cyanide at various oxygen concentrations by nitrogenase from Azotobacter vinelandii was measured with a well-defined system. Oxygen inhibited the reduction of each substrate uncompetitively. The inhibition constants (K(i)) were 0.014, 0.023, 0.008, and 0.003 atm of oxygen for reduction of nitrogen, acetylene, azide, and cyanide, respectively. The...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 183 23 شماره
صفحات -
تاریخ انتشار 2001