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Low-temperature Raman spectroscopy reveals small chromophore distortion in primary photointermediate of
Tomotsumi Fujisawa1, Masahiro Abe1, Jun Tamogami2
1Department of Chemistry and Applied Chemistry, Graduate School of Science and Engineering, Saga University, Japan.
Abstract:
Proteorhodopsin (PR) is a microbial rhodopsin functioning as a light-driven proton pump in aquatic bacteria. We performed low-temperature Raman measurements of PR to obtain the structure of the primary photoproduct, the K intermediate (PRK ). PRK showed the hydrogen-out-of-plane modes that are much less intense than those of bacteriorhodopsin as the prototypical light-driven proton pump from haloarchaea. The present results reveal the significantly relaxed chromophore structure in PRK , which can be coupled to the slow kinetics of the K intermediate. This structure suggests that PR transports protons using the small energy storage within the chromophore at the start of its photocycle.
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