Abstract
Measurements of difference spectra at increasing times after photoexcitation allowed calculation of the component spectra and the kinetics of the bacteriorhodopsin photocycle. The data are consistent with a single reaction sequence which includes reversible internal proton transfer reactions and two consecutive M states in which the retinal Schiff base is deprotonated. Mechanistically, the latter correspond to the switch of the proton pump; it is the immediate site for coupling the transformations of the chromophore to proton transport. It includes a protein conformational change and at pH ≥ 5.8 proton release on the extracellular side. At pH ≤ 5.8 proton release is delayed until later in the cycle. Proton uptake on the cytoplasmic side appears to depend on recovery of the initial protein conformation.
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Lanyi, J.K. (1992). From Time-Resolved Difference Spectra to Kinetics, Mechanism, and Thermodynamics in the Bacteriorhodopsin Photocycle. In: Pullman, A., Jortner, J., Pullman, B. (eds) Membrane Proteins: Structures, Interactions and Models. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 25. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2718-9_8
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DOI: https://doi.org/10.1007/978-94-011-2718-9_8
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