Methodology of pulsed photoacoustics and its application to probe photosystems and receptors

Sensors (Basel). 2010;10(6):5642-67. doi: 10.3390/s100605642. Epub 2010 Jun 3.

Abstract

We review recent advances in the methodology of pulsed time-resolved photoacoustics and its application to studies of photosynthetic reaction centers and membrane receptors such as the G protein-coupled receptor rhodopsin. The experimental parameters accessible to photoacoustics include molecular volume change and photoreaction enthalpy change. Light-driven volume change secondary to protein conformational changes or electrostriction is directly related to the photoreaction and thus can be a useful measurement of activity and function. The enthalpy changes of the photochemical reactions observed can be measured directly by photoacoustics. With the measurement of enthalpy change, the reaction entropy can also be calculated when free energy is known. Dissecting the free energy of a photoreaction into enthalpic and entropic components may provide critical information about photoactivation mechanisms of photosystems and photoreceptors. The potential limitations and future applications of time-resolved photoacoustics are also discussed.

Keywords: photoacoustics; photoactivation; photosynthesis; receptor; rhodopsin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Biosensing Techniques / instrumentation*
  • Biosensing Techniques / methods
  • Humans
  • Models, Biological
  • Photoacoustic Techniques / instrumentation*
  • Photoacoustic Techniques / methods*
  • Photosynthetic Reaction Center Complex Proteins / analysis*
  • Photosynthetic Reaction Center Complex Proteins / chemistry
  • Photosynthetic Reaction Center Complex Proteins / metabolism
  • Receptors, Cell Surface / analysis*
  • Receptors, Cell Surface / chemistry
  • Rhodopsin / analysis
  • Rhodopsin / chemistry
  • Rhodopsin / metabolism

Substances

  • Photosynthetic Reaction Center Complex Proteins
  • Receptors, Cell Surface
  • Rhodopsin