Resonance Raman study of intermediates of the halorhodopsin photocycle |
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| Institution: | 1. >Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg, D-3400 Göttingen, FRG;2. Max-Planck-Institut für Biochemie, D-8033 Martinsried, FRG |
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| Abstract: | The resonance Raman (RR) study of the retinal protein halorhodopsin (HR578) was extended to two of its photoproducts: HR and HRL410 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 HRL410 a deprotonated Schiff base in the 13-cis configuration. |
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