Table of Contents
Laser Chemistry
Volume 19 (1999), Issue 1-4, Pages 195-199

Electronic and Vibrational Coherence in Photosynthetic Cofactors: Comparison of Solutions and Proteins

1Department of Chemistry, University of Pennsylvania, Philadelphia 19104, PA, USA
2Department of Biochemistry and Biophysics and Johnson Foundation, University of Pennsylvania, Philadelphia 19104, PA, USA
3Department of Chemistry, The James Franck Institute, University of Chicago, Chicago 60637, IC, USA

Received 7 April 1997

Copyright © 1999 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The interaction between photosynthetic cofactors and the surrounding bath or protein environment is addressed via experimental measurements of the optical coherence responses from bacteriochlorophylla (Bchla) chromophores within the photosynthetic reaction center (RC) of Rhodobacter sphaeroides and solutions of Bchla monomers in THF and pyridine. The results indicate that both the spectrum of fluctuations and chromophore bath coupling strengths vary between solutions and protein. In particular, the protein environment yields faster dephasing, faster spectral diffusion, and significantly more inhomogeneity than solutions.