NDLI: Interpretation of the spatial charge displacements in bacteriorhodopsin in terms of structural changes during the photocycle.

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Interpretation of the spatial charge displacements in bacteriorhodopsin in terms of structural changes during the photocycle.

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Interpretation of the spatial charge displacements in bacteriorhodopsin in terms of structural changes during the photocycle.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Oroszi, L. Tóth-boconádi, R. Stoeckenius, W. Zimányi, L. Dér, A. Kulcsár, A. Keszthelyi, L. Ormos, P.
Description	Author Affiliation: Dér A ( Institute of Biophysics, Biological Research Center of the Hungarian Academy of Sciences, P.O. Box 521, Szeged H-6701, Hungary. derandra@everx.szbk.u-szeged.hu);
Abstract	We have recently introduced a method, made possible by an improved orienting technique using a combination of electric and magnetic fields, that allows the three-dimensional detection of the intramolecular charge displacements during the photocycle of bacteriorhodopsin. This method generates electric asymmetry, a prerequisite for the detection of electric signal on the macroscopic sample, in all three spatial dimensions. Purple membrane fragments containing bacteriorhodopsin were oriented so that their permanent electric dipole moment vectors were perpendicular to the membrane plane and pointed in the same direction. The resulting cylindrical symmetry was broken by photoselection, i. e., by flash excitation with low intensity linearly polarized light. From the measured electric signals, the three-dimensional motion of the electric charge center in the bacteriorhodopsin molecules was calculated for the first 400 microseconds. Simultaneous absorption kinetic recording provided the time-dependent concentrations of the intermediates. Combining the two sets of data, we determined the discrete dipole moments of intermediates up to M. When compared with the results of current molecular dynamics calculations, the data provided a decisive experimental test for selecting the optimal theoretical model for the proton transport and should eventually lead to a full description of the mechanism of the bacteriorhodopsin proton pump.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	96
Language	English
Publisher	National Academy of Sciences
Publisher Date	1999-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriorhodopsins Chemistry Electrochemistry Photosynthesis Models, Biological Proton Pumps Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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