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Biophys Chem. 1994 May;50(1-2):191-201.

Comparative studies on ion pumps of the bacterial rhodopsin family.

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  • 1Department of Biology, School of Science, Nagoya University, Japan.


Bacteriorhodopsin (proton pump), halorhodopsin (anion pump), sensory rhodopsin and phoborhodopsin (photosensors) are found in Halobacterium salinarium (halobium). In some other strains, other sets of rhodopsin pumps and sensors have been found. Here, these bacterial rhodopsins are classified according to their amino acid sequence homologies, and their host genera are assigned on the basis of 16S rRNA sequence comparison. Haloarcula is the host for cruxrhodopsins and a new genus (temporarily "Halorubra") is the host for archaerhodopsins. Difference in the all-trans:13-cis ratios of retinal in two proton pumps (bacteriorhodopsin and archaerhodopsin-2) at equilibrium states in the dark was ascribed to only one amino acid residue in the retinal pocket. This predicted methionine-145 in bacteriorhodopsin was point-mutated to phenylalanine as in archaerhodopsin-2. The mutated bacteriorhodopsin (M145F) became to show the same dark-adapted isomer ratio that archaerhodopsin-2 shows. Chimeric proton pumps were made by exchanging genes of one or more helix regions of two similar pumps (archaerhodopsin-1 and -2) in order to know structural delicacy of the inter-helix space. Preliminary results show that some photochemical properties depend on one helix or one distinct amino acid residue on the helix. Such new lines initiated by our archaerhodopsins are discussed for studying structure and function of these unique bacterial rhodopsins.

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