Damiano E, Bassilana M, Leblanc G
Eur J Biochem. 1985 Apr 1;148(1):183-8. doi: 10.1111/j.1432-1033.1985.tb08823.x.
The effects of chemical modifications of the Na+-H+ antiport in Escherichia coli have been analyzed by studying the resulting variations of the energy-dependent, downhill Na+ efflux from membrane vesicles. The histidyl reagent diethylpyrocarbonate (EtO)2C2O3 prevents the activation of the Na+ efflux mechanism by delta microH+ or its components. Inactivation of the antiporter by (EtO)2C2O3 is completely reversed by hydroxylamine. The data suggest that histidine residues are involved in the molecular mechanism of the Na+-H+ antiport. In contrast, no conclusive evidence suggesting participation of carboxylic, tyrosine or sulfhydryl residues in the Na+-H+ exchange reaction has been obtained.
通过研究膜囊泡中能量依赖性的、顺浓度梯度的钠离子外流的变化，分析了大肠杆菌中钠离子-氢离子反向转运体化学修饰的影响。组氨酸试剂焦碳酸二乙酯（(EtO)₂C₂O₃）可阻止由ΔμH⁺或其组分引起的钠离子外流机制的激活。(EtO)₂C₂O₃使反向转运体失活后可被羟胺完全逆转。数据表明，组氨酸残基参与了钠离子-氢离子反向转运的分子机制。相比之下，尚未获得确凿证据表明羧基、酪氨酸或巯基残基参与了钠离子-氢离子交换反应。
