The proton‐translocating ATPase of Escherichia coli
The proton‐translocating ATPase of Escherichia coli
复制标题
大肠杆菌的质子转位 ATP 酶
DOI:
10.1016/0014-5793(74)80880-x
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发表时间:
1974
期刊:
影响因子:
3.5
通讯作者:
P. Mitchell
中科院分区:
文献类型:
--
作者:
I. West;P. Mitchell
It was postulated by Mitchell [1, 2] that the ATPase systems of mitochondrial cristae membranes, chloroplast grana membranes and bacterial plasma membranes perform an essential bioenergetic function by coupling the reversible hydrolysis of ATP to the translocation of protons across the membrane. Direct observation of proton translocation by appropriate pH measurements during ATP hydrolysis was subsequently reported for mitochondria [3-5]~ chloroplast grana [6] and chromatophores from photosynthetic bacteria [7]. However, in spite of the important and suggestive work of Harold [8], the proton-translocating property of the ATPases of non-photosynthetic bacteria does not yet seem to have been directly demonstrated. In the absence of this crucial information, students of bacterial ATPase systems have unfortunately tended to regard an easily-dissociable water-soluble fragment of these systems (corresponding to the F, component of mitochondrial and chloroplast ATPases [9]) as the ‘pure ATPase’or simply as ‘the ATPase’.. The present paper attempts to encourage more functionally relevant studies of bacterial ATPase systems by showing, with direct pH measurements, that protons are translocated during the DCCD-sensitive hydrolysis of ATP by membrane vesicles prepared from Escherichia coli.* Present address: Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 IQW, UK Abbreviations: DCCD: dicyclohexylcarbodi-imide; FCCP: carbonylcyanide p-trifluoromethoxyphenylhydrazone; pHo-1ogro (chemical activity of H+ ions in the outer aqueous phase);-+ H+/P: proton translocation quotient giving number of protons translocated per ATP molecule hydrolysed.