Dynamics of energy transfer from lycopene to bacteriochlorophyll in genetically-modified LH2 complexes of Rhodobacter sphaeroides

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title = "Dynamics of energy transfer from lycopene to bacteriochlorophyll in genetically-modified LH2 complexes of Rhodobacter sphaeroides",
abstract = "LH2 complexes from Rb. sphaeroides were modified genetically so that lycopene, with I I saturated double bonds, replaced the native carotenoids which contain 10 saturated double bonds. Tuning the S, level of the carotenoid in LH2 in this way affected the dynamics of energy transfer within LH2, which were investigated using both steady-state and time-resolved techniques. The S I energy of lycopene in n-hexane was determined to be similar to12 500 +/- 150 cm(-1), by direct measurement of the S-1-S-2 transient absorption spectrum using a femtosecond IR-probing technique, thus placing an upper limit on the S, energy of lycopene in the LH2 complex. Fluorescence emission and excitation spectra demonstrated that energy can be transferred from lycopene to the bacteriochlorophyll molecules within this LH2 complex. The energy-transfer dynamics within the mutant complex were compared to wild-type LH2 from Rb. sphaeroides containing the carotenoid spheroidene and from Rs. molischian1l7n, in which lycopene is the native carotenoid. The results show that the overall efficiency for Crt --> B850 energy transfer is similar to80{\%} in lyco-LH2 and similar to95{\%} in WT-LH2 of Rb. sphaeroides. The difference in overall Crt --> BChl transfer efficiency of lyco-LH2 and WT-LH2 mainly relates to the low efficiency of the Crt S-1 --> BChl pathway for complexes containing lycopene, which was 20{\%} in lyco-LH2. These results show that in an LH2 complex where the Crt Si energy is sufficiently high to provide efficient spectral overlap with both B800 and B850 Q(y) states, energy transfer via the Crt S, state occurs to both pigments. However, the introduction of lycopene into the Rb. sphaeroides LH2 complex lowers the S-1 level of the carotenoid sufficiently to prevent efficient transfer of energy to the B 800 Q, state, leaving only the Crt S-1 --> B 850 channel, strongly suggesting that Crt S-1 --> BChl energy transfer is controlled by the relative Crt S-1 and BChl Q(y) energies.",
author = "Helena Billsten and Jennifer Herek and G Garcia-Asua and L Hash{\o}j and Tomas Polivka and CN Hunter and Villy Sundstr{\"o}m",
note = "The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Chemical Physics (S) (011001060)",
year = "2002",
doi = "10.1021/bi011741v",
language = "English",
volume = "41",
pages = "4127--4136",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "The American Chemical Society (ACS)",
number = "12",