On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin

A. G. Doukas; A. Pande; T. Suzuki; R. H. Callender; B. Honig; M. Ottolenghi

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

Zuckerman Institute

Résultat de recherche › examen par les pairs

32 Citations (Scopus)

Résumé

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.

Langue d'origine	English
Pages (de-à)	275-279
Nombre de pages	5
Journal	Biophysical Journal
Volume	33
Numéro de publication	2
DOI	https://doi.org/10.1016/S0006-3495(81)84889-8
Statut de publication	Published - 1981

Financement

Bailleurs de fonds	Numéro du bailleur de fonds
City College	PCM80-1093 1
City University
National Science Foundation	PCM79-02683
National Institutes of Health	EY03142

ASJC Scopus Subject Areas

Biophysics

Accès au document

10.1016/S0006-3495(81)84889-8

Autres fichiers et liens

Citer

Doukas, A. G., Pande, A., Suzuki, T., Callender, R. H., Honig, B., & Ottolenghi, M. (1981). On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin. Biophysical Journal, 33(2), 275-279. https://doi.org/10.1016/S0006-3495(81)84889-8

@article{842598d432334dd1b657a109918fe268,

title = "On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin",

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.",

author = "Doukas, {A. G.} and A. Pande and T. Suzuki and Callender, {R. H.} and B. Honig and M. Ottolenghi",

note = "Funding Information: This work was supported in part by the National Science Foundation (PCM79-02683), by the National Institutes of Health (EY03142), by a City University PSC-BHE Faculty Award at the City College, and by the National Science Foundation (PCM80-1093 1) at the University of Illinois.",

year = "1981",

doi = "10.1016/S0006-3495(81)84889-8",

language = "English",

volume = "33",

pages = "275--279",

journal = "Biophysical Journal",

issn = "0006-3495",

publisher = "Biophysical Society",

number = "2",

}

TY - JOUR

T1 - On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin

AU - Doukas, A. G.

AU - Pande, A.

AU - Suzuki, T.

AU - Callender, R. H.

AU - Honig, B.

AU - Ottolenghi, M.

N1 - Funding Information: This work was supported in part by the National Science Foundation (PCM79-02683), by the National Institutes of Health (EY03142), by a City University PSC-BHE Faculty Award at the City College, and by the National Science Foundation (PCM80-1093 1) at the University of Illinois.

PY - 1981

Y1 - 1981

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0019378003&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019378003&partnerID=8YFLogxK

U2 - 10.1016/S0006-3495(81)84889-8

DO - 10.1016/S0006-3495(81)84889-8

M3 - Article

AN - SCOPUS:0019378003

SN - 0006-3495

VL - 33

SP - 275

EP - 279

JO - Biophysical Journal

JF - Biophysical Journal

IS - 2

ER -

On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin

Résumé

Financement

ASJC Scopus Subject Areas

Accès au document

Autres fichiers et liens

Empreinte numérique

Citer