X-ray crystallography of bacteriorhodopsin and its photointermediates: insights into the mechanism of proton transport.
In the last few years, detailed structural information from high-resolution x-ray diffraction has been added to the already large body of spectroscopic and mutational data on the bacteriorhodopsin proton transport cycle. Although there are still many gaps, it is now possible to reconstruct the main events in the translocation of the proton and how they are coupled to the photoisomerization of the retinal chromophore. Future structural work will concentrate on describing the details of the individual proton transfer steps during the photocycle.
Lanyi
J K
JK
Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA. jlanyi@orion.oac.uci.edu
D001436:Bacteriorhodopsins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation
D001436:Bacteriorhodopsins