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Biophysical Journal 33: 275-279 (1981)
© 1981 the Biophysical Society

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On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin.

A G Doukas, A Pande, T Suzuki, R H Callender, B Honig and M Ottolenghi

ABSTRACT

Continuous-flow resonance Raman experiments carried out in bacteriorhodopsin show that the exchange of a deuteron on the Schiff base with a proton takes place in times shorter than 3 ms. Exchange mechanisms based on a base-catalyzed deprotonation followed by reprotonation of the Schiff base are excluded. A mechanism is suggested in which a water molecule interacts directly with the Schiff base deuteron in a concerted exchange mechanism. It appears that in the dark, the binding site is more accessible to neutral water molecules than to charged protons.




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I. Rousso, I. Brodsky, A. Lewis, and M. Sheves
The Role of Water in Retinal Complexation to Bacterio-opsin
J. Biol. Chem., June 9, 1995; 270(23): 13860 - 13868.
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Copyright © 1981 by the Biophysical Society.