Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics

IUBMB Life. 2013 Mar;65(3):247-54. doi: 10.1002/iub.1134.

Abstract

In this article, we discuss single molecule observation of rotational catalysis by E. coli ATP synthase (F-ATPase) using small gold beads. Studies involving a low viscous drag probe showed the stochastic properties of the enzyme in alternating catalytically active and inhibited states. The importance of subunit interaction between the rotor and the stator, and thermodynamics of the catalysis are also discussed. "Single Molecule Enzymology" is a new trend for understanding enzyme mechanisms in biochemistry and physiology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism*
  • Biocatalysis
  • Catalytic Domain
  • Escherichia coli / chemistry
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Gold / chemistry
  • Hydrolysis
  • Molecular Dynamics Simulation
  • Molecular Motor Proteins / chemistry*
  • Molecular Motor Proteins / metabolism
  • Protein Conformation
  • Protein Subunits / chemistry*
  • Protein Subunits / metabolism
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / metabolism
  • Protons*
  • Rotation
  • Thermodynamics

Substances

  • Escherichia coli Proteins
  • Molecular Motor Proteins
  • Protein Subunits
  • Protons
  • Gold
  • Adenosine Triphosphate
  • Proton-Translocating ATPases