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The molecular structure of the Na + ‐translocating F 1 F 0 ‐ATPase of Acetobacterium woodii , as revealed by electron microscopy, resembles that of H + ‐translocating ATPases
Author(s) -
Reidlinger Jutta,
Mayer Frank,
Müller Volker
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01222-9
Subject(s) - atpase , chemistry , electron microscope , electron transport chain , crystallography , biophysics , enzyme , biology , biochemistry , physics , optics
The Na + ‐translocating F 1 F 0 ‐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 α 3 β 3 structure, and the F 1 F 0 complex had molecular dimensions very similar to those of H + ‐translocating ATPases of E. coli , chloroplasts, and mitochondria.