Picosecond time-resolved absorption and fluorescence in the bacteriorhodopsin photocycle: Vibrationally-excited species

Blanchard, Dominique; Gilmore, D. A.; Brack, T. L.; Lemaire, Henri; Hughes, D. G.; Atkinson, Gordon

doi:10.1016/0301-0104(91)89050-k

Cited by 20 publications

(35 citation statements)

References 36 publications

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“…Timeresolved measurements reveal that fluorescence from K*-590 appears with the same -3.5-ps time constant found via absorption (9,13). The maximum of the K*-590 fluorescence spectrum is blue-shifted by "17 nm relative to BR*-570 and K*-590 has a 2-fold higher fluorescence yield (13,14).…”

mentioning

confidence: 80%

“…The maximum of the K*-590 fluorescence spectrum is blue-shifted by "17 nm relative to BR*-570 and K*-590 has a 2-fold higher fluorescence yield (13,14). No fluorescence has been associated with J-625 (9,13). …”

mentioning

confidence: 93%

“…Fluorescence spectroscopy has been utilized to characterize the initial BR photocycle intermediates (9,13,14). Timeresolved measurements reveal that fluorescence from K*-590 appears with the same -3.5-ps time constant found via absorption (9,13).…”

mentioning

confidence: 99%

“…Involving changes in the retinal chromophore, the protein, and/or interactions between the two, these primary molecular events occur within femto/picoseconds of optical excitation in BR and, therefore, encompass the optically populated FranckCondon (FC) (H) and vibrationally relaxed (I) levels of the excited electronic state of BR-570 (BR*-570). In addition, the J and K photochemical intermediates, having absorption maxima near 625 nm and 590 nm, respectively, are formed within the initial 10 ps (4)(5)(6)(7)(8)(9). Transient absorption data have shown that (i) BR*-570(H) decays to BR*-570(I) in 100-200 fs (7,8), (ii) BR*-570(I) decays directly to the J intermediate within an "500-fs time constant (4)(5)(6)(7), and (iii) the J intermediate decays to form Kwith an -3.5-ps time constant (5,6,9).…”

mentioning

confidence: 99%

“…The earliest stages of the molecular mechanism by which light energy is stored by BR is of particular importance (2)(3)(4)(5)(6)(7)(8)(9). Involving changes in the retinal chromophore, the protein, and/or interactions between the two, these primary molecular events occur within femto/picoseconds of optical excitation in BR and, therefore, encompass the optically populated FranckCondon (FC) (H) and vibrationally relaxed (I) levels of the excited electronic state of BR-570 (BR*-570).…”

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confidence: 99%

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Primary picosecond molecular events in the photoreaction of the BR5.12 artificial bacteriorhodopsin pigment.

Delaney

Brack

Atkinson

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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The picosecond dynamics of the photoreaction of an artificial bacteriorhodopsin (BR) pigment containing a retinal in which a five-membered ring spans the C-12 to C-14 positions of the polyene chain (BR5.12) is examined by using time-resolved absorption and fluorescence and resonance Raman spectroscopy. The ring within the retinal chromophore of BR5.12 blocks the C-13=C-14 isomerization proposed to be a primary step in the energy storage /transduction mechanism in the BR photocycle. Relative to the native BR pigment (BR-570), the absorption spectrum of BR5.12 is red-shifted by 8 nm. The fluorescence spectrum of BR5.12 closely resembles that of BR-570 although the relative fluorescence yield is higher ("10-fold

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confidence: 80%

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confidence: 93%