Low-temperature single-molecule spectroscopy on photosynthetic pigment-protein complexes from purple bacteria

Photosynth Res. 2009 Aug-Sep;101(2-3):171-9. doi: 10.1007/s11120-009-9450-2. Epub 2009 Jun 20.

Abstract

The primary reactions of purple bacterial photosynthesis take place within two well characterized pigment-protein complexes, the core Reaction Center-Light Harvesting 1 (RC-LH1) complex and the more peripheral Light Harvesting 2 (LH2) complex. These antenna complexes serve to absorb incident solar radiation and to transfer it to the reaction-centers, where it is used to 'power' the photosynthetic redox reaction. This review provides an overview of how the character of the electronically excited states of these pigment-protein complexes are determined by quantum mechanics and how the respective spectral signatures can be observed by single-molecule spectroscopy.

Publication types

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

MeSH terms

  • Photosynthesis / physiology*
  • Pigments, Biological / chemistry
  • Pigments, Biological / metabolism*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism*
  • Proteobacteria / metabolism*
  • Spectrum Analysis / methods*
  • Temperature*

Substances

  • Pigments, Biological
  • Plant Proteins