Energy transduction in the sodium F-ATPase of Propionigenium modestum

P Dimroth; H Wang; M Grabe; G Oster

doi:10.1073/pnas.96.9.4924

Energy transduction in the sodium F-ATPase of Propionigenium modestum

Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4924-9. doi: 10.1073/pnas.96.9.4924.

Authors

P Dimroth¹, H Wang, M Grabe, G Oster

Affiliation

¹ Mikrobiologisches Institut, Eidgenössische Technische Hochschule, ETH-Zentrum, Schmelzbergstrasse 7, CH-8092 Zürich, Switzerland.

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.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Bacterial Proteins / chemistry
Energy Transfer
Escherichia coli / chemistry
Gram-Negative Anaerobic Bacteria / enzymology*
Molecular Motor Proteins*
Protein Conformation
Proton-Translocating ATPases / chemistry*

Substances

Bacterial Proteins
Molecular Motor Proteins
Proton-Translocating ATPases