Relationships between nitrogenase, glutamine synthetase, glutamine, and energy charge in Azotobacter vinelandii
Relationships between nitrogenase, glutamine synthetase, glutamine, and energy charge in Azotobacter vinelandii
复制标题
维氏固氮菌固氮酶、谷氨酰胺合成酶、谷氨酰胺与能量电荷之间的关系
作者:
J. Kleinschmidt;D. Kleiner
When continuous cultures of Azotobacter vinelandii were supplied with ammonium or nitrate in amounts, which just repressed nitrogenase synthesis completely, both the intracellular glutamine level and the degree of adenylylation of the glutamine synthetase (GS) increased only slightly (from 0.45–0.50 mM and from 2 to 3 respectively), while the total GS level remained unaffected. Higher amounts of ammonium additionally inhibited the nitrogenase activity, caused a strong rise in the intracellular glutamine concentration and adenylylation of the GS, but caused no change in the ATP/ADP ratio. These results are considered as evidence that in A. vinelandii the regulation of nitrogenase synthesis is not linked to the adenylylation state of the GS and to the intracellular glutamine level, and that the inhibition of the nitrogenase activity as a consequence of a high extracellular ammonium level is not mediated via a change in the energy charge.