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PMID: 2554293 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 20 ·1989-10-00 ·Pages 7876-9

Dencher NA, Dresselhaus D, Zaccai G, Büldt G

Abstract

A neutron diffraction study of spectroscopic states for the light-energized proton pump bacteriorhodopsin (BR) is presented. The photocycle states BR-568 and M were generated at temperatures above 4 degrees C and were measured after trapping at--180 degrees C. In the BR-568 to M-state transition, which is known to be a key step in transmembrane proton pumping, reversible structural changes of the protein were detected. These structural alterations occur in the neighborhood of the cyclohexene ring and at the Schiff's base end of the chromophore retinal. They are interpreted as a 1-2 degree tilt of three or four of the transmembrane alpha-helices or as positional changes of four or five amino acids. The structural changes observed are inherent in the transport mechanism of bacteriorhodopsin.

MeSH Terms
Bacteriorhodopsins/metabolism Fourier Analysis Halobacterium/metabolism Light Neutrons Protein Conformation Protons Scattering, Radiation
Chemicals
Protons Bacteriorhodopsins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Dencher N A
Department of Physics/Biophysics, Freie Universität Berlin, Federal Republic of Germany.
Dresselhaus D
Zaccai G
Büldt G
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.20.7876
Published
1989-10-00
Pages
7876-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC298174
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.86.20.7876 PMC Full Text View journal details
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