Conformational Analysis of a Retinal Schiff Base Chromophore in Proteorhodopsin by Raman Optical Activity

Raman optical activity (ROA) spectroscopy was used to study the conformation of the retinal Schiff base chromophore in green-light-absorbing proteorhodopsin, which is a globally distributed light-driven proton pump of aquatic bacteria. The ROA spectrum consisted mostly of the negative vibrational bands of the chromophore, while the hydrogen out-of-plane mode (at 960 cm(-1)) appeared as the sole positive band. This distinct spectral feature was not explained by the twisted structure of the retinal Schiff base but was reproduced by the structural model in which the polyene chain on the beta-ionone ring side was bent out-of-plane. The bent chromophore structure potentially couples with proton pumping through the motion of the sixth helix in contact with the beta-ionone ring.

Automated summary

ROA spectroscopy was used to study the conformation of the retinal Schiff base chromophore in green-light-absorbing proteorhodopsin, revealing that the chromophore structure potentially couples with proton pumping through the motion of the sixth helix. This unique spectral feature was not explained by the twisted structure of the retinal Schiff base but was reproduced by a structural model with a bent polyene chain on the beta-ionone ring side.