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. 1981 Feb;33(2):275–279. doi: 10.1016/S0006-3495(81)84889-8

On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin.

A G Doukas, A Pande, T Suzuki, R H Callender, B Honig, M Ottolenghi
PMCID: PMC1327428  PMID: 7225508

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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