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Annu Rev Physiol. 2004;66:665-88.

Bacteriorhodopsin.

Author information

  • Department of Physiology and Biophysics, University of California, Irvine, California 92697, USA. jlanyi@orion.oac.uci.edu

Abstract

Fourier transform infrared and Raman spectroscopy, solid-state NMR, and X-ray crystallography have contributed detailed information about the structural changes in the proton transport cycle of the light-driven pump, bacteriorhodopsin. The results over the past few years add up to a step-by-step description of the configurational changes of the photoisomerized retinal, how these changes result in internal proton transfers and the release of a proton to the extracellular surface and uptake on the other side, as well as the conservation and transformation of excess free energy during the cycle.

PMID:
14977418
[PubMed - indexed for MEDLINE]
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