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Energy transduction in the sodium F-ATPase of Propionigenium modestum.


ABSTRACT: The F-ATPase of the bacterium Propionigenium modestum is driven by an electrochemical sodium gradient between the cell interior and its environment. Here we present a mechanochemical model for the transduction of transmembrane sodium-motive force into rotary torque. The same mechanism is likely to operate in other F-ATPases, including the proton-driven F-ATPases of Escherichia coli.

SUBMITTER: Dimroth P 

PROVIDER: S-EPMC21793 | biostudies-literature | 1999 Apr

REPOSITORIES: biostudies-literature

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Energy transduction in the sodium F-ATPase of Propionigenium modestum.

Dimroth P P   Wang H H   Grabe M M   Oster G G  

Proceedings of the National Academy of Sciences of the United States of America 19990401 9


The F-ATPase of the bacterium Propionigenium modestum is driven by an electrochemical sodium gradient between the cell interior and its environment. Here we present a mechanochemical model for the transduction of transmembrane sodium-motive force into rotary torque. The same mechanism is likely to operate in other F-ATPases, including the proton-driven F-ATPases of Escherichia coli. ...[more]

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