Sensitivity of the retinal circular dichroism of bacteriorhodopsin to the mutagenetic single substitution of amino acids: tyrosine

FEBS Letters

Stern, Lawrence J.¹  Gobind Khorana, H.¹  Mogi, Tatsushi¹  El-Sayed, M.A.² 

[1] Departments of Chemistry and Biology, MIT, Cambridge, MA 02139, USA;Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024, USA

关键词: Bacteriorhodopsin;    Circular dichroism;    Exiton interaction;    Protein conformation;    Purple membrane;    Site-specific mutant;    bR;    bacteriorhodopsin;    ebR;    wild-type bR expressed in E. coli;    Y185F;    mutant bR expressed in E. coli in which Tyr-185 is substituted by Phe;   

DOI  :  10.1016/0014-5793(90)80178-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bacteriorhodopsin (bR) in the native purple membrane, in wild type expressed in E. coli and reconstituted in lipid vesicles, and its constituted mutants with substitutions of Tyr-185 by Phe all are found to have different visible retinal CD spectra. The results strongly suggest that the environment of the retinal in bR determines the sign and heterogeneity of its visible retinal CD spectrum. This supports the recent proposal that the observed biphasic CD spectrum of bR is due to the superposition of the CD spectra having opposite signs of more than one type of bR rather than due to exciton coupling.

【 授权许可】

Unknown