Bacteriorhodopsin.

J K Lanyi; H Luecke

doi:10.1016/s0959-440x(00)00226-8

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PubMed · 11495732

Bacteriorhodopsin.

J K Lanyi·H Luecke

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Abstract

High-resolution maps from X-ray diffraction of bacteriorhodopsin and some of its photointermediates have yielded insights into how the isomerization of the bound retinal drives ion transport. Although important mechanistic details are still undecided, the events of the photochemical cycle are now understood to reflect changes in specific hydrogen bonds of protein groups and bound water molecules in response to motions of the retinal chain.

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Bacteriorhodopsins Ion Transport Isomerism Light Membrane Proteins Models, Structural Protein Conformation Proton Pumps Purple Membrane Retinaldehyde Water X-Ray Diffraction Journal Article Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.Review

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J K Lanyi, H Luecke. 2001. Bacteriorhodopsin.. https://doi.org/10.1016/s0959-440x(00)00226-8

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