Energy transduction in the sodium F-ATPase of Propionigenium modestum.
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.
Dimroth
P
P
Mikrobiologisches Institut, Eidgenössische Technische Hochschule, ETH-Zentrum, Schmelzbergstrasse 7, CH-8092 Zürich, Switzerland.
Wang
H
H
Grabe
M
M
Oster
G
G
D001426:Bacterial Proteins / Q000737:chemistry; D004735:Energy Transfer; D004926:Escherichia coli / Q000737:chemistry; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology*; D020409:Molecular Motor Proteins; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry*
D001426:Bacterial Proteins; D020409:Molecular Motor Proteins; D006180:Proton-Translocating ATPases