Feedback inhibition of nitrogenase
نویسندگان
چکیده
منابع مشابه
Feedback inhibition of nitrogenase.
No inhibition of nitrogenase activity by physiological levels of NH4+ or carbamyl phosphate was observed in extracts of Azotobacter vinelandii. All of the 15N2 reduced by cultures which received no NH4+ was found in the cells. By contrast, more than 95% of the 15N2 reduced by cultures which had been given NH4+ was found in the medium. Failure to examine the culture medium would lead to the erro...
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...
متن کاملInhibition of nitrogenase activity by ammonium chloride in Azotobacter vinelandii.
In Azotobacter vinelandii cells, the short-term inhibition of nitrogenase activity by NH4Cl was found to depend on several factors. The first factor is the dissolved oxygen concentration during the assay of nitrogenase. When cells are incubated with low concentrations of oxygen, nitrogenase activity is low and ammonia inhibits strongly. With more oxygen, nitrogenase activity increases. Cells in...
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A novel, pulse-modulated spectroscopic system for measuring fractional leghemoglobin oxygenation and infected cell O(2) concentration (O(i)) in intact attached nodules of soybean (Glycine max) is described. The system is noninvasive and uses a pulsed (1000 Hertz) light-emitting diode coupled to an optical fiber to illuminate the nodule with light at 660 nanometer. A second optical fiber receive...
متن کاملConcerted Feedback Inhibition
Concerted feedback inhibition of aspartokinase activity from Pseudomonasfluorescens by the combination of L-threonine and r.-lysine, or by L-threonine and L-methionine was freely and rapidly reversible. Inhibition by L-threonine, or by the concerted pairs of amino acids was kinetically “mixed” with respect to L-aspartate and noncompetitive with regard to ATP. In the presence of L-threonine the ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1981
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.148.3.884-888.1981