Femtosecond dynamics of energy transfer in B800-850 light-harvesting complexes of Rhodobacter sphaeroides.
We report femtosecond transient absorption studies of energy transfer dynamics in the B800-850 light-harvesting complex (LHC) of Rhodobacter sphaeroides 2.4.1. For complexes solubilized in lauryldimethylamine-N-oxide (LDAO), the carotenoid to bacteriochlorophyll (Bchl) B800 and carotenoid to Bchl B850 energy transfer times are 0.34 and 0.20 ps, respectively. The B800 to B850 energy transfer time is 2.5 ps. For complexes treated with lithium dodecyl sulfate (LDS), a carotenoid to B850 energy transfer time of less than or equal to 0.2 ps is seen, and a portion of the total carotenoid population is decoupled from Bchl. In both LDAO-solubilized and LDS-treated complexes an intensity-dependent picosecond decay component of the excited B850 population is ascribed to excitation annihilation within minimal units of the LHC.
Trautman
J K
JK
Department of Chemistry, Cornell University, Ithaca, NY 14853.
Shreve
A P
AP
Violette
C A
CA
Frank
H A
HA
Owens
T G
TG
Albrecht
A C
AC
D001429:Bacteriochlorophylls / Q000378:metabolism; D002338:Carotenoids / Q000378:metabolism; D002734:Chlorophyll / Q000378:metabolism*; D004735:Energy Transfer; D007700:Kinetics; D007834:Lasers; D008027:Light; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins / Q000378:metabolism*; D012242:Rhodobacter sphaeroides / Q000378:metabolism*; D013053:Spectrophotometry; D013997:Time Factors
D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D002734:Chlorophyll; D002338:Carotenoids