| Abstract |
Optimum temperature and pH of glutamine synthetase activity (E.C. 3.6.1.2.) of R. sphaeroides D-230 was 35℃ and 6.8, respectively. The adenylated state of GS in R. sphaeroides D-230 was stabilized by addition of 0.2mg/ml of cethyltrimethylammoniumbromide. Valine, histidine, proline, isoleucine, and lysine were good nitrogen source for the growth of R. sphaeroides D-230. The growth of R. sphaeroides D-230 in N₂, NaNO₃or NH₄Cl as sole nitrogen source was lower than in any other culture conditions. GS activity was inhibited, more or less, by various amino acid. The relative inhibition rate of the enzyme by added 7mM arginine, NH₄Cl, N₂, and NaNO₃was 63.8%, 26.79%, 6.24%, and 10.64%, respectively. The hydrogen evolution of R. sphaeroides D-230 grown in N-limited media was inhibited by 0.1mM MSX, irreversible GS inhibitor. GS activity was completely inhibited by 1.0mM MSX but ammonia released maximally at the same concentration of MSX. Ammonia release by added MSX was increased up to 1.0mM MS, but decreased above 1.0mM MSX. It is probably due to inhibition of nitrogenase actixity by MSX. Nitrogenase activity was not inhibited at low concentration of MSX. These results suggests that the inhibition of nitrogenase activity by ammonia is mediated by products of ammonia assimilation rather than by ammonia itself. |
