Time-resolved spectroscopy of energy transfer and trapping upon selective excitation in membranes of Heliobacillus mobilis at low temperature.
Transient absorption difference spectra in the Qy absorption band of bacteriochlorophyll (BChl) g and in the 670 nm absorption band of the primary acceptor A0 in membranes of Heliobacillus mobilis (Hc. mobilis) were measured at 20 K upon selective excitation at 668, 793, 810, and 815 nm with a 5 nm spectral bandwidth. When excited at 793 nm, the spectral equilibration of excitations from shorter to longer wavelength-absorbing pigments occurred within 3 ps and mostly localized at the band centered around 808 nm. When excited at 668 nm, the excitation energy transfer from the 670 nm absorbing pigment to the Qy band of BChl g took less than 0.5 ps, and the energy redistribution occurred and localized at 808 nm as in the case of the 793 nm excitation. All of the excitations were localized at the long wavelength pigment pool centered around 810 or 813 nm when excited at 810 or 815 nm. A slower energy transfer process with a time constant of 15 ps was also observed within the pool of long wavelength-absorbing pigments upon selective excitation at different wavelengths as has been observed by Lin et al. (Biophys. J. 1994, 67, 2479) when excited at 590 nm. Energy transfer from long wavelength antenna molecules to the primary electron donor P798 followed by the formation of P+ took place with a time constant of 55-70 ps for all excitations. Direct excitation of the primary electron acceptor A0, which absorbed at 670 nm, showed the same kinetic behavior as in the case when different forms of antenna pigments were excited in the Qy region. This observation generally supports the trapping-limited case of energy transfer in which the excitations have high escape probability from the reaction center (RC) until the charge separation takes place. Possible mechanisms to account for the apparent "uphill" energy transfer from the long wavelength antenna pigments to P798 are discussed.
Chiou
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HC
Department of Chemistry and Biochemistry, Arizona State University, Tempe 85287-1604, USA.
Lin
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S
Blankenship
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RE
D001419:Bacteria / Q000378:metabolism* / Q000528:radiation effects; D001429:Bacteriochlorophylls / Q000235:genetics / Q000378:metabolism* / Q000528:radiation effects; D055592:Biophysical Phenomena; D001703:Biophysics; D004579:Electron Transport; D004735:Energy Transfer; D007700:Kinetics; D008027:Light; D045342:Light-Harvesting Protein Complexes; D008566:Membranes / Q000378:metabolism / Q000528:radiation effects; D010777:Photochemistry; D010788:Photosynthesis / Q000502:physiology; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism* / Q000528:radiation effects; D013053:Spectrophotometry; D013696:Temperature
D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins