TY - JOUR
T1 - Ultrafast spectroscopy of the protonated Schiff bases of free and C13=C14 locked retinals
AU - Hou, B.
AU - Friedman, N.
AU - Ruhman, S.
AU - Sheves, M.
AU - Ottolenghi, M.
PY - 2001/7/26
Y1 - 2001/7/26
N2 - In this study, the ultrafast pump-probe spectroscopy of the all-trans protonated Schiff base of retinal (trans-PSB) in solution, is compared to that of two retinal analogues, trans-PSB5.12 and 13-cis-PSB5.13, in which C13=C14 torsional motion is inhibited by a rigid five-membered ring structure. The objective is to obtain measures of internal conversion (IC) dynamics in these polyenes. Contrasting the results with those obtained for the same pigments when attached to their opsin protein, serve to appreciate the protein role in catalyzing energy transduction in bacteriorhodopsin. Several major features appear to be common to all three PSBs: (i) A 50-100 fs process due to a primary relaxation out of the Franck-Condon (FC) region, (ii) A subsequent biexponential decay (t1 = 1-2 ps and t2 = 4-7 ps) of the fluorescent state (FS) assumed to be due to IC, and (iii) Spectral modulations in the FS emission. The three are only marginally effected by locking of the C13=C14 bond. With respect to features (i) and (iii) the PSB model compounds behave analogously to the related retinal protein bacteriorhodopsin (bR). However, this does not apply to the FS decay. While in bR, the IC takes place with a 0.5 ps decay time, locking of the C13=C14 bond in bR markedly increases the FS lifetime to ∼ 15 ps. These observations demonstrate the crucial role played by the protein in directing the isomerization action to the active double bond and enhancing the rate of IC. They also prove that these coordinates are not exclusive pathways of IC in the isolated PSB of retinal. The mechanism of ground-state repopulation in the PSBs is discussed in light of these results.
AB - In this study, the ultrafast pump-probe spectroscopy of the all-trans protonated Schiff base of retinal (trans-PSB) in solution, is compared to that of two retinal analogues, trans-PSB5.12 and 13-cis-PSB5.13, in which C13=C14 torsional motion is inhibited by a rigid five-membered ring structure. The objective is to obtain measures of internal conversion (IC) dynamics in these polyenes. Contrasting the results with those obtained for the same pigments when attached to their opsin protein, serve to appreciate the protein role in catalyzing energy transduction in bacteriorhodopsin. Several major features appear to be common to all three PSBs: (i) A 50-100 fs process due to a primary relaxation out of the Franck-Condon (FC) region, (ii) A subsequent biexponential decay (t1 = 1-2 ps and t2 = 4-7 ps) of the fluorescent state (FS) assumed to be due to IC, and (iii) Spectral modulations in the FS emission. The three are only marginally effected by locking of the C13=C14 bond. With respect to features (i) and (iii) the PSB model compounds behave analogously to the related retinal protein bacteriorhodopsin (bR). However, this does not apply to the FS decay. While in bR, the IC takes place with a 0.5 ps decay time, locking of the C13=C14 bond in bR markedly increases the FS lifetime to ∼ 15 ps. These observations demonstrate the crucial role played by the protein in directing the isomerization action to the active double bond and enhancing the rate of IC. They also prove that these coordinates are not exclusive pathways of IC in the isolated PSB of retinal. The mechanism of ground-state repopulation in the PSBs is discussed in light of these results.
UR - http://www.scopus.com/inward/record.url?scp=0035954989&partnerID=8YFLogxK
U2 - 10.1021/jp0034980
DO - 10.1021/jp0034980
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AN - SCOPUS:0035954989
SN - 1089-5647
VL - 105
SP - 7042
EP - 7048
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 29
ER -