Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes

J Bioenerg Biomembr. 2007 Dec;39(5-6):435-9. doi: 10.1007/s10863-007-9114-x.

Abstract

The abundance of E. coli F1-ATPase molecules observed to rotate using gold nanorods attached to the gamma-subunit was quantitated. Individual F1 molecules were determined to be rotating based upon time dependent fluctuations of red and green light scattered from the nanorods when viewed through a polarizing filter. The average number of F1 molecules observed to rotate in the presence of GTP, ATP, and without nucleotide was approximately 50, approximately 25, and approximately 4% respectively. In some experiments, the fraction of molecules observed to rotate in the presence of GTP was as high as 65%. These data indicate that rotational measurements made using gold nanorods provide information of the F1-ATPase mechanism that is representative of the characteristics of the enzyme population as a whole.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Escherichia coli Proteins*
  • Gold
  • Metal Nanoparticles
  • Microscopy
  • Molecular Motor Proteins
  • Molecular Probe Techniques*
  • Molecular Probes*
  • Nanotechnology / methods
  • Nanotubes*
  • Proton-Translocating ATPases / analysis
  • Proton-Translocating ATPases / metabolism*
  • Rotation

Substances

  • Escherichia coli Proteins
  • Molecular Motor Proteins
  • Molecular Probes
  • Gold
  • Proton-Translocating ATPases