From Femtoseconds To Biology: Mechanism Of The Light-Driven Proton Pump In Bacteriorhodopsin

Richard A. Mathies; Johan Lugtenburg; Charles V. Shank

doi:10.1117/12.951656

8 May 1989 From Femtoseconds To Biology: Mechanism Of The Light-Driven Proton Pump In Bacteriorhodopsin

Richard A. Mathies, Johan Lugtenburg, Charles V. Shank

Proceedings Volume 1057, Biomolecular Spectroscopy; (1989) https://doi.org/10.1117/12.951656
Event: OE/LASE '89, 1989, Los Angeles, CA, United States

Abstract

Femtosecond time-resolved absorption and time-resolved resonance Raman spectroscopy are used to examine the molecular mechanism of the light-driven proton pump in bacteriorhodopsin. Transient absorption spectroscopy with 6-fs pulses is used to directly observe the excited-state, double bond torsional isomerization of the retinal chromophore. Time-resolved resonance Raman spectroscopy is used to determine the structure of the retinal prosthetic group in each of the subsequent photolytic intermediates. Based on these results, a new "C-T Model" for the molecular mechanism of the proton pump has been developed. The key feature of this model is an isomerization-driven conformational change of the protein from the T-form to the C-form which acts as a "reprotonation switch" and stores energy to drive later events in the photocycle.

Citation Download Citation

Richard A. Mathies, Johan Lugtenburg, and Charles V. Shank "From Femtoseconds To Biology: Mechanism Of The Light-Driven Proton Pump In Bacteriorhodopsin", Proc. SPIE 1057, Biomolecular Spectroscopy, (8 May 1989); https://doi.org/10.1117/12.951656

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