Energy transduction in the sodium F-ATPase of Propionigenium modestum
AUTOR(ES)
Dimroth, Peter
FONTE
The National Academy of Sciences
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=21793Documentos Relacionados
- Nucleotide sequence of the F0 subunits of the sodium dependent F1F0 ATPase of Propionigenium modestum.
- The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase
- Genetic and Biochemical Characterization of the F-ATPase Operon from Streptococcus sanguis 10904
- The F-ATPase Operon Promoter of Streptococcus mutans Is Transcriptionally Regulated in Response to External pH
- Sequence of subunits a and b of the sodium ion translocating adenosine triphosphate synthase of Propionigenium modestum.