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.