期刊论文详细信息
FEBS Letters | |
Resonance Raman study of intermediates of the halorhodopsin photocycle | |
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 HRL 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 HRL 410 a deprotonated Schiff base in the 13-cis configuration.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020289355ZK.pdf | 733KB | download |