Ultrafast time-resolved carotenoid to-bacteriochlorophyll energy transfer in LH2 complexes from photosynthetic bacteria.
Steady-state and ultrafast time-resolved optical spectroscopic investigations have been carried out at 293 and 10 K on LH2 pigment-protein complexes isolated from three different strains of photosynthetic bacteria: Rhodobacter (Rb.) sphaeroides G1C, Rb. sphaeroides 2.4.1 (anaerobically and aerobically grown), and Rps. acidophila 10050. The LH2 complexes obtained from these strains contain the carotenoids, neurosporene, spheroidene, spheroidenone, and rhodopin glucoside, respectively. These molecules have a systematically increasing number of pi-electron conjugated carbon-carbon double bonds. Steady-state absorption and fluorescence excitation experiments have revealed that the total efficiency of energy transfer from the carotenoids to bacteriochlorophyll is independent of temperature and nearly constant at approximately 90% for the LH2 complexes containing neurosporene, spheroidene, spheroidenone, but drops to approximately 53% for the complex containing rhodopin glucoside. Ultrafast transient absorption spectra in the near-infrared (NIR) region of the purified carotenoids in solution have revealed the energies of the S1 (2(1)Ag-)-->S2 (1(1)Bu+) excited-state transitions which, when subtracted from the energies of the S0 (1(1)Ag-)-->S2 (1(1)Bu+) transitions determined by steady-state absorption measurements, give precise values for the positions of the S1 (2(1)Ag-) states of the carotenoids. Global fitting of the ultrafast spectral and temporal data sets have revealed the dynamics of the pathways of de-excitation of the carotenoid excited states. The pathways include energy transfer to bacteriochlorophyll, population of the so-called S* state of the carotenoids, and formation of carotenoid radical cations (Car*+). The investigation has found that excitation energy transfer to bacteriochlorophyll is partitioned through the S1 (1(1)Ag-), S2 (1(1)Bu+), and S* states of the different carotenoids to varying degrees. This is understood through a consideration of the energies of the states and the spectral profiles of the molecules. A significant finding is that, due to the low S1 (2(1)Ag-) energy of rhodopin glucoside, energy transfer from this state to the bacteriochlorophylls is significantly less probable compared to the other complexes. This work resolves a long-standing question regarding the cause of the precipitous drop in energy transfer efficiency when the extent of pi-electron conjugation of the carotenoid is extended from ten to eleven conjugated carbon-carbon double bonds in LH2 complexes from purple photosynthetic bacteria.
Cong
Hong
H
Department of Chemistry, University of Connecticut, U-3060, 55 North Eagleville Road, Storrs, Connecticut 06269-3060, USA.
Niedzwiedzki
Dariusz M
DM
Gibson
George N
GN
LaFountain
Amy M
AM
Kelsh
Rhiannon M
RM
Gardiner
Alastair T
AT
Cogdell
Richard J
RJ
Frank
Harry A
HA
D000465:Algorithms; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D001429:Bacteriochlorophylls / Q000737:chemistry*; D002338:Carotenoids / Q000737:chemistry*; D003080:Cold Temperature; D004735:Energy Transfer; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D012242:Rhodobacter sphaeroides / Q000737:chemistry* / Q000502:physiology; D012241:Rhodopseudomonas / Q000737:chemistry* / Q000502:physiology; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D019265:Spectroscopy, Near-Infrared; D013696:Temperature; D013997:Time Factors
C081521:B800-850 light-harvesting complex, bacteria; D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; C005637:spheroidene; C104880:spheroidenone; D002338:Carotenoids; C008604:neurosporene