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F 0 and F 1 parts of ATP synthases from Clostridium thermoautotrophicum and Escherichia coli are not functionally compatible
Author(s) -
Das Amaresh,
Ljungdahl Lars G.
Publication year - 1993
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(93)81482-f
Subject(s) - escherichia coli , atp synthase , clostridium , chemistry , adenosine triphosphate , escherichia coli proteins , biochemistry , microbiology and biotechnology , bacteria , biology , enzyme , gene , genetics
F 1 ‐stripped membrane vesicles from Clostridium thermoautotrophicum and Escherichia coli were reconstituted with F 1 ‐ATPases from both bacteria. Reconstituted F i F o ‐ATPase complexes were catalytically active, i.e. capable of hydrolyzing ATP. Homologous‐type ATPase complexes having F 0 and F 1 parts of ATP synthases from the same origin were DCCD sensitive and supported ATP‐driven enhancement ofanilinonaphthalene sulfonate (ANS) fluorescence. Hybrid‐type ATPase complexes having F 0 and F 1 parts of ATP synthases from different origins were neither DCCD sensitive nor did they support ATP‐driven enhancement of ANS fluorescence. Analyzing these results it has been demonstrated that the F 0 and F 1 parts of ATP synthases of these two bacteria are not functionally compatible.