Resonance Raman study of intermediates of the halorhodopsin photocycle

FEBS Letters

Oesterhelt, D.¹  Diller, R.²  Tittor, J.¹  Stockburger, M.² 

[1] Max-Planck-Institut für Biochemie, D-8033 Martinsried, FRG;>Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg, D-3400 Göttingen, FRG

关键词: Resonance Raman spectroscopy;    Photocycle;    Light-driven chloride pump;    Retinal isomerization;    Retinal protein;   

DOI  :  10.1016/0014-5793(87)80682-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The resonance Raman (RR) study of the retinal protein halorhodopsin (HR₅₇₈) was extended to two of its photoproducts: HR and HR^L ₄₁₀ RR spectra of both species were recorded in H₂O and D₂O and compared with the RR spectra of the intermediates L₅₅₀ and M₄₁₂ from the bacteriorhodopsin photocycle. HR₅₂₀ was found to be a protonated Schiff base in the 13-cis configuration and HR^L ₄₁₀ a deprotonated Schiff base in the 13-cis configuration.

【 授权许可】

Unknown