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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.

The Journal of Physical Chemistry Letters
|November 6, 2025
PubMed
Summary
This summary is machine-generated.

This study reveals how freshwater xanthorhodopsins (XRs) adapt to acidic conditions by enhancing light-harvesting efficiency. Protonation of specific amino acids boosts energy transfer between carotenoids and retinal, optimizing light capture in changing aquatic environments.

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Area of Science:

  • Biochemistry
  • Spectroscopy
  • Quantum Chemistry

Background:

  • Microbial rhodopsins are crucial for light harvesting in aquatic ecosystems.
  • Xanthorhodopsins (XRs) uniquely utilize both retinal and carotenoids for light capture.
  • Understanding XR adaptation to environmental pH is vital for aquatic biochemistry.

Purpose of the Study:

  • Investigate the pH-dependent energy transfer efficiency in a novel freshwater XR, Kin4B8.
  • Elucidate the molecular mechanisms behind altered lutein-to-retinal excitation-energy transfer (EET) under acidic conditions.
  • Determine the role of specific amino acid protonation states in modulating XR function.

Main Methods:

  • Spectroscopic measurements to analyze light absorption and energy transfer.
  • Quantum chemical calculations to model electronic coupling and spectral overlap.
  • pH-dependent analysis of XR behavior, focusing on key residues His60 and Asp94.

Main Results:

  • Kin4B8 exhibits increased lutein-to-retinal EET efficiency from 40% to 55% under acidic pH.
  • Protonation of Asp94 significantly enhances lutein-retinal electronic coupling.
  • Despite spectral redshift, enhanced coupling compensates for reduced overlap, increasing EET rate by 1.07-fold.

Conclusions:

  • Protonation of Asp94 is a key mechanism for pH-responsive tuning of EET in xanthorhodopsins.
  • Rhodopsin-carotenoid complexes adapt to varying light environments through pH-dependent energy transfer modulation.
  • This study provides insights into the adaptive strategies of light-harvesting proteins in diverse aquatic habitats.