Water as a cofactor in the unidirectional light-driven proton transfer steps in bacteriorhodopsin.

Photochemistry and Photobiology
Akio MaedaT Ebrey

Abstract

Recent evidence for involvement of internal water molecules in the mechanism of bacteriorhodopsin is reviewed. Water O-H stretching vibration bands in the Fourier transform IR difference spectra of the L, M and N intermediates of bacteriorhodopsin were analyzed by photoreactions at cryogenic temperatures. A broad vibrational band in L was shown to be due to formation of a structure of water molecules connecting the Schiff base to the Thr46-Asp96 region. This structure disappears in the M intermediate, suggesting that it is involved in transient stabilization of the L intermediate prior to proton transfer from the Schiff base to Asp85. The interaction of the Schiff base with a water molecule is restored in the N intermediate. We propose that water is a critical mobile component of bacteriorhodopsin, forming organized structures in the transient intermediates during the photocycle and, to a large extent, determining the chemical behavior of these transient states.

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Citations

Aug 29, 2009·Journal of Molecular Biology·Masataka YamamotoTsutomu Kouyama
Oct 22, 2008·Journal of Molecular Biology·Naoki HayakawaTsutomu Kouyama
Dec 8, 2009·Journal of Molecular Biology·Tsutomu KouyamaKunio Ihara
Feb 12, 2013·Structure·Ting WangMarc T Facciotti
Nov 21, 2007·Biochimica Et Biophysica Acta·Michael F BrownIngrid Wallat

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Methods Mentioned

BETA
X-ray
infrared spectroscopy
neutron diffraction
NMR
irradiating

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