ON THE MECHANISM OF H+ TRANSLOCATION BY MITOCHONDRIAL H+-ATPASE - STUDIES WITH CHEMICAL MODIFIER OF TYROSINE RESIDUES
ON THE MECHANISM OF H+ TRANSLOCATION BY MITOCHONDRIAL H+-ATPASE - STUDIES WITH CHEMICAL MODIFIER OF TYROSINE RESIDUES
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DOI：
10.1007/bf00744279
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发表时间：
1984-01-01
影响因子：
3
通讯作者：
PAPA, S
中科院分区：
文献类型：
--
作者：
GUERRIERI, F;YAGI, A;PAPA, S
详细研究了四硝基甲烷硝化酪氨酸残基对H+-ATPase复合体催化的亚线粒体颗粒、解偶联颗粒和纯化的复合体的H+传导和其他反应的影响。亚线粒体颗粒经四硝基甲烷处理后，可显著抑制H+-ATPase复合体的ATP水解、ATP-33PI交换和质子传导。这些效应是由H+-ATPase复合体的酪氨酸残基硝化引起的，表现为在360 nm处出现吸收峰(专用于硝基酪氨酸的形成)，并抑制了从四硝基甲烷处理的颗粒中提纯的复合体中的ATP水解和ATP-33PI交换。四硝基甲烷处理也抑制了镶嵌有FO的磷脂小泡的H+传导。显然，FO的酪氨酸残基(S)在ATPase复合体中参与了与能量相关的质子转运。
A detailed study of the effect of nitration of Tyr residues by tetranitromethane on H+ conduction and other reactions catalyzed by the H+-ATPase complex in phosphorylating submitochondrial particles, uncoupled particles and the purified complex is presented. Tetranitromethane treatment of submitochondrial particles results in marked inhibition of ATP hydrolysis, ATP-33Pi exchange, and proton conduction by the H+-ATPase complex. These effects are caused by nitration of Tyr residues of H+-ATPase complex as shown by the appearance of the absorption peak at 360 nm (specific for nitrotyrosine formation) and inhibition of ATP hydrolysis and ATP-33Pi exchange in the complex purified from tetranitromethane-treated particles. H+ conduction in phospholipid vesicles inlaid with FO is also inhibited by tetranitromethane treatment. Apparently Tyr residue(s) of FO are critically involved in energy-linked proton translocation in the ATPase complex.