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    • From femtoseconds to biology: Mechanism of bacteriorhodopsin’s light-driven proton pump

      Richard A Mathies

      Volume 103 Issue 3 March 1991 pp 283-293

    • Fulltext

       

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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jcsc/103/03/0283-0293

    • Keywords

       

      Purple membrane; femtosecond spectroscopy; resonance Raman spectroscopy; nonstationary state spectroscopy

    • Abstract

       

      Bacteriorhodopsin is a retinal-containing protein that functions as a light-driven proton pump. Resonance Raman and femtosecond dynamic absorption spectroscopy are being used to elucidate the molecular mechanism of bacteriorhodopsin. The primary photochemical process is atrans- to-cis isomerization about the C13=C14 bond of the retinal chromophore that has been directly observed using femtosecond dynamic absorption spectroscopy. The excited state isomerization dynamics can be quantitatively analyzed using a new theory for nonstationary state spectroscopy. Resonance Raman vibrational spectroscopy has been used to determine the structure of the chromophore in each of bacteriorhodopsin’s intermediates and to analyze the kinetics of the photocycle. These results are integrated into an explicit molecular model (the C-T Model) for proton pumping in bacteriorhodopsin.

    • Author Affiliations

       

      Richard A Mathies1

      1. Chemistry Department, University of California, Berkeley, CA - 94720, USA

    • Dates

       
      Published
      March 1991

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