| SMITH, Andrea, Martin TOUL, Daniel PLUSKAL, Racha BAATALLAH, Glwadys GAGNOT, José Gaspar RANGEL PAMPLONA PIZARRO PINTO, Vinicius T. T. SANTANA, Markéta STUCHLÁ, Petr NEUGEBAUER, Pimchai CHAIYEN, Jiří DAMBORSKÝ, David BEDNÁŘ, Yves L. L. JANIN, Zbyněk PROKOP and Martin MAREK. Catalytic mechanism for Renilla-type luciferases. Nature Catalysis. Nature Portfolio, 2023, vol. 6, No 1, p. 23-38. ISSN 2520-1158. Available from: https://dx.doi.org/10.1038/s41929-022-00895-z. |
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@article{2285204,
author = {Smith, Andrea and Toul, Martin and Pluskal, Daniel and Baatallah, Racha and Gagnot, Glwadys and Rangel Pamplona Pizarro Pinto, José Gaspar and Santana, Vinicius T. T. and Stuchlá, Markéta and Neugebauer, Petr and Chaiyen, Pimchai and Damborský, Jiří and Bednář, David and Janin, Yves L. L. and Prokop, Zbyněk and Marek, Martin},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41929-022-00895-z},
keywords = {CYPRIDINA LUCIFERIN; PROTEIN CRYSTALLIZATION; BIOLUMINESCENCE; RENIFORMIS; LIGHT; CHEMILUMINESCENCE; COELENTERAZINE; STABILITY; LUMINESCENCE; SPECIFICITY},
language = {eng},
issn = {2520-1158},
journal = {Nature Catalysis},
title = {Catalytic mechanism for Renilla-type luciferases},
url = {https://www.nature.com/articles/s41929-022-00895-z},
volume = {6},
year = {2023}
}
TY - JOUR
ID - 2285204
AU - Smith, Andrea - Toul, Martin - Pluskal, Daniel - Baatallah, Racha - Gagnot, Glwadys - Rangel Pamplona Pizarro Pinto, José Gaspar - Santana, Vinicius T. T. - Stuchlá, Markéta - Neugebauer, Petr - Chaiyen, Pimchai - Damborský, Jiří - Bednář, David - Janin, Yves L. L. - Prokop, Zbyněk - Marek, Martin
PY - 2023
TI - Catalytic mechanism for Renilla-type luciferases
JF - Nature Catalysis
VL - 6
IS - 1
SP - 23-38
EP - 23-38
PB - Nature Portfolio
SN - 25201158
KW - CYPRIDINA LUCIFERIN
KW - PROTEIN CRYSTALLIZATION
KW - BIOLUMINESCENCE
KW - RENIFORMIS
KW - LIGHT
KW - CHEMILUMINESCENCE
KW - COELENTERAZINE
KW - STABILITY
KW - LUMINESCENCE
KW - SPECIFICITY
UR - https://www.nature.com/articles/s41929-022-00895-z
N2 - The widely used coelenterazine-powered Renilla luciferase was discovered over 40 years ago, but the oxidative mechanism by which it generates blue photons remains unclear. Here we decipher Renilla-type catalysis through crystallographic, spectroscopic and computational experiments. Structures of ancestral and extant luciferases complexed with the substrate-like analogue azacoelenterazine or a reaction product were obtained, providing molecular snapshots of coelenterazine-to-coelenteramide oxidation. Bound coelenterazine adopts a Y-shaped conformation, enabling the deprotonated imidazopyrazinone component to attack O-2 via a radical charge-transfer mechanism. A high emission intensity is secured by an aspartate from a conserved proton-relay system, which protonates the excited coelenteramide product. Another aspartate on the rim of the catalytic pocket fine-tunes the electronic state of coelenteramide and promotes the formation of the blue light-emitting phenolate anion. The results obtained also reveal structural features distinguishing flash-type from glow-type bioluminescence, providing insights that will guide the engineering of next-generation luciferase-luciferin pairs for ultrasensitive optical bioassays.
ER -
SMITH, Andrea, Martin TOUL, Daniel PLUSKAL, Racha BAATALLAH, Glwadys GAGNOT, José Gaspar RANGEL PAMPLONA PIZARRO PINTO, Vinicius T. T. SANTANA, Markéta STUCHLÁ, Petr NEUGEBAUER, Pimchai CHAIYEN, Jiří DAMBORSKÝ, David BEDNÁŘ, Yves L. L. JANIN, Zbyněk PROKOP and Martin MAREK. Catalytic mechanism for Renilla-type luciferases. \textit{Nature Catalysis}. Nature Portfolio, 2023, vol.~6, No~1, p.~23-38. ISSN~2520-1158. Available from: https://dx.doi.org/10.1038/s41929-022-00895-z.
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