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
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
收藏
页码:17 / 20
页数:4
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