Paul T D, Ludden P W
Biochem J. 1984 Dec 15;224(3):961-9. doi: 10.1042/bj2240961.
Adenine nucleotide pools were measured in Rhodospirillum rubrum cultures that contained nitrogenase. The average energy charge [([ATP] + 1/2[ADP])/([ATP] + [ADP] + [AMP])] was found to be 0.66 and 0.62 in glutamate-grown and N-limited cultures respectively. Treatment of glutamate-grown cells with darkness, ammonia, glutamine, carbonyl cyanide m-chlorophenylhydrazone, or phenazine methosulphate resulted in perturbations in the adenine nucleotide pools, and led to loss of whole-cell nitrogenase activity and modification in vivo of the Fe protein. Treatment of N-limited cells resulted in similar changes in adenine nucleotide pools but not enzyme modification. No correlations were found between changes in adenine nucleotide pools or ratios of these pools and switch-off of nitrogenase activity by Fe protein modification in vivo. Phenazine methosulphate inhibited whole-cell activity at low concentrations. The effect on nitrogenase activity was apparently independent of Fe protein modification.
对含有固氮酶的深红红螺菌培养物中的腺嘌呤核苷酸库进行了测定。在以谷氨酸生长的培养物和氮限制培养物中,平均能荷[([ATP] + 1/2[ADP])/([ATP] + [ADP] + [AMP])]分别为0.66和0.62。用黑暗、氨、谷氨酰胺、羰基氰化物间氯苯腙或吩嗪硫酸甲酯处理以谷氨酸生长的细胞,会导致腺嘌呤核苷酸库受到扰动,并导致全细胞固氮酶活性丧失以及铁蛋白在体内发生修饰。处理氮限制细胞会导致腺嘌呤核苷酸库发生类似变化,但不会引起酶的修饰。在体内,腺嘌呤核苷酸库的变化或这些库的比率与通过铁蛋白修饰关闭固氮酶活性之间未发现相关性。吩嗪硫酸甲酯在低浓度下会抑制全细胞活性。对固氮酶活性的影响显然与铁蛋白修饰无关。