Electrical power fuels rotary ATP synthase

Structure. 2003 Dec;11(12):1469-73. doi: 10.1016/j.str.2003.11.011.

Abstract

ATP synthesis by F-type ATP synthases consumes energy stored in a transmembrane electrochemical gradient of protons or sodium ions. The electric component of the ion motive force is crucial for ATP synthesis. Here, we incorporate recent results on structure and function of the F(0) domain and present a mechanism for torque generation with the fundamental nature of the membrane potential as driving force in the core.

Publication types

  • Review

MeSH terms

  • Bacterial Proton-Translocating ATPases / chemistry*
  • Bacterial Proton-Translocating ATPases / metabolism*
  • Electrochemistry
  • Escherichia coli / enzymology
  • Ions
  • Models, Biological
  • Models, Molecular
  • Molecular Motor Proteins
  • Protein Structure, Tertiary
  • Sodium / chemistry
  • Structure-Activity Relationship

Substances

  • Ions
  • Molecular Motor Proteins
  • Sodium
  • Bacterial Proton-Translocating ATPases