Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction

Journal Article · Sun Oct 01 04:00:00 EDT 1989 · Proceedings of the National Academy of Sciences of the United States of America; (USA)

DOI:https://doi.org/10.1073/pnas.86.20.7876· OSTI ID:5047248

Dencher, N A; Dresselhaus, D; Zaccai, G; Bueldt, G ^[1]

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1. Freie Universitaet Berlin (Germany, F.R.)

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{degree}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.

• OSTI ID: 5047248
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:20; ISSN 0027-8424; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BARYONS
CELL CONSTITUENTS
CELL MEMBRANES
COHERENT SCATTERING
DIFFRACTION
ELEMENTARY PARTICLES
FERMIONS
FOURIER ANALYSIS
HADRONS
MEMBRANE TRANSPORT
MEMBRANES
NEUTRON DIFFRACTION
NEUTRONS
NUCLEONS
ORGANIC COMPOUNDS
PHOTOSYNTHETIC BACTERIA
PIGMENTS
PROTEIN STRUCTURE
PROTEINS
PROTONS
RHODOPSIN
SCATTERING