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- W200051829 abstract "Publisher Summary This chapter describes the spectroscopic and chemical properties of a great variety of chromophore species, included are chromophores equilibrating with the purple complex, intermediates of the reconstitution reaction, reduced chromophores, and chromophores containing retinal analogs. The chapter discusses the structure of the retinal binding site in bacteriorhodopsin and properties of the retinal binding site in bacteriorhodopsin. Both all-trans and 13-cis retinal are able to form a purple complex. The reconstitution occurs via intermdiate chromophores. In both types of purple complexes, 13-cis/all-trans isomerisation is catalyzed by the protein moiety under certain conditions. The last step of the reconstitution reaction is blocked for the 11-cis isomer. Apparently, this isomer is able to interact only with those amino acid residues that are responsible for the formation of the 400 nm and the 430/460 nm intermediate chromophores. The phenomenon of energy transfer between aromatic amino acids and the retinyl moiety has been observed in various reduced chromophores." @default.
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- W200051829 date "1978-01-01" @default.
- W200051829 modified "2023-09-27" @default.
- W200051829 title "RETINAL-PROTEIN INTERACTION IN BACTERIORHODOPSIN" @default.
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- W200051829 doi "https://doi.org/10.1016/b978-0-08-022626-2.50016-x" @default.
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