Structural mechanism governing radiationless energy transfer in Renilla bioluminescence
- 1Masaryk University
Abstract
The nonradiative transport of electronic excitation from one chromophore to another, known as resonance energy transfer, lies at the root of photochemical processes in biology. Unlike photosynthesis, bioluminescence converts chemical energy into light through an enzymatic oxygenation of an energy-rich luciferin. In glowing cnidarians, the energy is relocated from an excited oxyluciferin to a fluorescent protein, shifting the colour and enhancing the quantum yield of a photogenic reaction. How protein-chromophore complexes assemble during this interplay in real space, and what this association entails for function, are unknown. Here, we report co-crystal structures of a 120-kilodalton energy-transfer complex from the luminescent soft coral Renilla reniformis. We find a heterotetrameric 2:2 assembly composed of two coelenteramide-loaded luciferases (RrLuc) docked at opposite sides of a head-to-tail dimer of green fluorescent protein (RrGFP). The edge-to-edge distance between donor and acceptor chromophores is below 3 nm, favouring the Forster-type radiationless energy transfer. Furthermore, RrGFP serves not only as a colour-switchable antenna and luminescence amplifier but also tunes the efficiency of luciferase catalysis by controlling its inherent dynamics. Our results provide detailed spatial information about intermolecular dipole-dipole coupling in Renilla bioluminescence, including the arrangement of donor-acceptor pairs that secure excited-state energy transfer with exquisite precision.
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BibTeX
@misc{pluskal2026structural,
title = {{Structural mechanism governing radiationless energy transfer in Renilla bioluminescence}},
author = {D. Pluskal and M. Toul and N. Verma and A. Smrckova and T. Gao and T. Buryska and T. de Martines and J. Horackova and M. Stuchla and V. Novakova and M. Nemergut and Y. L. Janin and A. deMello and S. Stavrakis and M. Vacha and J. Damborsky and D. Bednar and L. Hernychova and Z. Prokop and M. Marek},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.01.748624},
url = {https://www.biorxiv.org/content/10.64898/2026.09.01.748624v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Structural mechanism governing radiationless energy transfer in Renilla bioluminescence
AU - D. Pluskal
AU - M. Toul
AU - N. Verma
AU - A. Smrckova
AU - T. Gao
AU - T. Buryska
AU - T. de Martines
AU - J. Horackova
AU - M. Stuchla
AU - V. Novakova
AU - M. Nemergut
AU - Y. L. Janin
AU - A. deMello
AU - S. Stavrakis
AU - M. Vacha
AU - J. Damborsky
AU - D. Bednar
AU - L. Hernychova
AU - Z. Prokop
AU - M. Marek
PY - 2026
DA - 2026/09/01
PB - bioRxiv
DO - 10.64898/2026.09.01.748624
UR - https://www.biorxiv.org/content/10.64898/2026.09.01.748624v1
AB - The nonradiative transport of electronic excitation from one chromophore to another, known as resonance energy transfer, lies at the root of photochemical processes in biology. Unlike photosynthesis, bioluminescence converts chemical energy into light through an enzymatic oxygenation of an energy-rich luciferin. In glowing cnidarians, the energy is relocated from an excited oxyluciferin to a fluorescent protein, shifting the colour and enhancing the quantum yield of a photogenic reaction. How protein-chromophore complexes assemble during this interplay in real space, and what this association entails for function, are unknown. Here, we report co-crystal structures of a 120-kilodalton energy-transfer complex from the luminescent soft coral Renilla reniformis. We find a heterotetrameric 2:2 assembly composed of two coelenteramide-loaded luciferases (RrLuc) docked at opposite sides of a head-to-tail dimer of green fluorescent protein (RrGFP). The edge-to-edge distance between donor and acceptor chromophores is below 3 nm, favouring the Forster-type radiationless energy transfer. Furthermore, RrGFP serves not only as a colour-switchable antenna and luminescence amplifier but also tunes the efficiency of luciferase catalysis by controlling its inherent dynamics. Our results provide detailed spatial information about intermolecular dipole-dipole coupling in Renilla bioluminescence, including the arrangement of donor-acceptor pairs that secure excited-state energy transfer with exquisite precision.
ER -