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Updated: Jan 12, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Protonation-Enhanced Energy Transfer in Xanthorhodopsin Kin4B8
Kazuhiro J Fujimoto1,2, Yuta A Tsuzuki2, Masae Konno3
1Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University, Furocho, Chikusa, Nagoya 464-8601, Japan.
None:
Microbial rhodopsins are key light-harvesting proteins for energy conversion in aquatic environments. While typically reliant on retinal, xanthorhodopsins (XRs) also employ carotenoids as antenna pigments. Here, we investigate Kin4B8, a novel freshwater XR that exhibits a counterintuitive increase in lutein-to-retinal excitation-energy transfer (EET) efficiency under acidic conditions─from 40% at neutral pH to 55%─despite a redshift in its absorption spectrum. By integrating spectroscopic measurements with quantum chemical calculations, we examine the influence of pH-dependent protonation states of two key residues, His60 and Asp94, on EET. We find that protonation of Asp94, in particular, markedly enhances lutein-retinal electronic coupling while moderately reducing spectral overlap. The 1.24-fold increase in squared coupling compensates for the decreased overlap, resulting in a net 1.07-fold increase in the EET rate. These findings suggest that rhodopsin-carotenoid complexes employ protonation-dependent tuning of carotenoid-retinal energy transfer as a mechanism for pH-responsive adaptation to diverse light environments.
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