Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1460, Issue 1, Pages 177-191Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0005-2728(00)00138-9
Keywords
hydrogen bond; Fourier transform infrared spectroscopy; O-H vibration; mutant; vectorial transport; switch
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Internal water molecules are considered to play a crucial role in the functional processes of proton pump proteins. They may participate in hydrogen-bonding networks inside proteins that constitute proton pathways, in addition, they could participate in the switch reaction by mediating an essential proton transfer at the active site. Nevertheless, little has been known about the structure and function of internal water molecules in such proteins. Recent progress in infrared spectroscopy and X-ray crystallography provided new information on water molecules inside bacteriorhodopsin, the light-driven proton pump. The accumulated knowledge on bacteriorhodopsin in the last decade of the 20th century will lead to a realistic picture of internal water molecules at work in the 21st century. In this review, I describe how the role of water molecules has been studied in bacteriorhodopsin, and what should be known about the role of water molecules in the future. (C) 2000 Elsevier Science B.V. All rights reserved.
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