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Bacteriorhodopsin's L sub 550 intermediate contains a C14-C15 s-trans-retinal chromophore

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)

Conformational changes of the retinal chromophore about the C14-C15 bond in bacteriorhodopsin (BR) have been proposed in models for the mechanism of light-driven proton transport. To determine the C14-C15 conformation in BR's L{sub 550} intermediate, the authors have examined the resonance Raman spectra of BR derivatives regenerated with retinal deuterated at the 14 and 15 positions. Vibrational calculations show that the C14-{sup 2}H and C15-{sup 2}H rocking modes form symmetric (A) and antisymmetric (B) combinations in (14,15-{sup 2}H)retinal chromophores. When there is a trans conformation about the single bond between C14 and C15 (14-s-trans), a small frequency separation or splitting is observed between the A and B modes. In addition, the monodeuterium rock should appear at an unusually low frequency in the 14-{sup 2}H-labeled 14-s-cis molecules. These patterns are insensitive to computational details. Time-resolved resonance Raman spectra were obtained of BR's L{sub 550} intermediate regenerated with (14-{sup 2}H)-, (15-{sup 2}H)- and (14,15-{sup 2}H)retinal. These results show that L{sub 550} contains a 14-s-trans chromophore and suggest that only 14-2-trans structures are involved in the proton pumping photocycle of BR.

OSTI ID:
6891634
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 85:7; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English