Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization | Zendy

Till Stensitzki | Zendy; Yonggang Yang | Zendy; Vera Muders | Zendy; Ramona Schlesinger | Zendy; Joachim Heberle | Zendy; Karsten Heyne | Zendy

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Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization

Author(s) -

Till Stensitzki,

Yonggang Yang,

Vera Muders,

Ramona Schlesinger,

Joachim Heberle,

Karsten Heyne

Publication year - 2016

Publication title -

structural dynamics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.415

H-Index - 29

ISSN - 2329-7778

DOI - 10.1063/1.4948338

Subject(s) - photoisomerization , photoexcitation , femtosecond , femtochemistry , photochemistry , isomerization , ultrafast laser spectroscopy , spectroscopy , infrared spectroscopy , chromophore , chemistry , infrared , materials science , laser , optics , excited state , atomic physics , physics , organic chemistry , quantum mechanics , catalysis , biochemistry

Vibrational dynamics of the retinal all- trans to 13- cis photoisomerization in channelrhodopsin-1 from Chlamydomonas augustae ( Ca ChR1) was investigated by femtosecond visible pump mid-IR probe spectroscopy. After photoexcitation, the transient infrared absorption of C-C stretching modes was detected. The formation of the 13- cis photoproduct marker band at 1193 cm −1 was observed within the time resolution of 0.3 ps. We estimated the photoisomerization yield to (60 ± 6) %. We found additional time constants of (0.55 ± 0.05) ps and (6 ± 1) ps, assigned to cooling, and cooling processes with a back-reaction pathway. An additional bleaching band demonstrates the ground-state heterogeneity of retinal.

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