The resonance Raman (RR) study of the retinal protein halorhodopsin (HR 578 ) was extended to two of its photoproducts: HR and HR L 410 RR spectra of both species were recorded in H 2 O and D 2 O and compared with the RR spectra of the intermediates L 550 and M 412 from the bacteriorhodopsin photocycle. HR 520 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.
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Diller et al. (1987) studied this question.
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