Polarized pump-probe spectroscopy of exciton transport in bacteriochlorophyll a- protein from Prosthecochloris aestuarii
The polarization of the Q/sub x/ electronic transition in the BChl a-protein complex from the green sulfur bacterium Prosthecochloris aestuarii was monitored by pump-probe spectroscopy with approx. 1.5-ps resolution at 598, 603, and 609 nm. At 603 nm, the polarization decays with a mean lifetime of 4.78 ps. Substantial residual polarization appears at long times (the ratio A/sub parallel//A/sub perpendicular/ of optical densities for probe pulses polarized parallel and perpendicular to the excitation pulse is approx. 1.7) in consequence of the nonrandom chromophore orientations. The polarized pump-probe transients have been analyzed in terms of an exciton hopping model that incorporates the known geometry of the BChl a-protein.
- Research Organization:
- Iowa State Univ., Ames (USA)
- DOE Contract Number:
- W-7405-ENG-82
- OSTI ID:
- 6206038
- Journal Information:
- J. Phys. Chem.; (United States), Vol. 92:23
- Country of Publication:
- United States
- Language:
- English
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37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
CHLOROPHYLL-BINDING PROTEINS
RYDBERG STATES
DYE LASERS
ELECTRONIC STRUCTURE
EXPERIMENTAL DATA
GAS DYNAMIC LASERS
PHOTOSYNTHETIC BACTERIA
POLARIZATION
TIME DEPENDENCE
DATA
ENERGY LEVELS
EXCITED STATES
GAS LASERS
INFORMATION
LASERS
LIQUID LASERS
NUMERICAL DATA
ORGANIC COMPOUNDS
PHOTOSYNTHETIC REACTION CENTERS
PROTEINS
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400500 - Photochemistry