THE MOLECULAR-STRUCTURE OF THE NA+-TRANSLOCATING F1F0-ATPASE OF ACETOBACTERIUM-WOODII, AS REVEALED BY ELECTRON-MICROSCOPY, RESEMBLES THAT OF H+-TRANSLOCATING ATPASES

被引：13

作者：

REIDLINGER, J ^{[1
]}

MAYER, F ^{[1
]}

MULLER, V ^{[1
]}

机构：

[1] UNIV GOTTINGEN,INST MIKROBIOL,D-37077 GOTTINGEN,GERMANY

来源：

FEBS LETTERS | 1994年 / 356卷 / 01期

关键词：

F1F0-ATPASE (EC 3.6.1.34); NA+-TRANSLOCATING; ELECTRON MICROSCOPY; ACETOGENIC BACTERIA;

D O I：

10.1016/0014-5793(94)01222-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Na+-translocating F1F0-ATPase of Acetobacterium woodii was examined by electron microscopy. After reconstitution into proteoliposomes, knobs typical for the F-1 domain were visible on the outside of the membrane. The F-1-part of the isolated enzyme showed a hexagonal symmetry suggesting an alpha(3) beta(3) structure, and the F1F0 complex had molecular dimensions very similar to those of H+-translocating ATPases of E. coli, chloroplasts, and mitochondria.

引用

页码：17 / 20

页数：4

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