Detailed Information on Publication Record
2023
Catalytic mechanism for Renilla-type luciferases
SMITH, Andrea, Martin TOUL, Daniel PLUSKAL, Racha BAATALLAH, Glwadys GAGNOT et. al.Basic information
Original name
Catalytic mechanism for Renilla-type luciferases
Authors
SMITH, Andrea (703 Slovakia, belonging to the institution), Martin TOUL (203 Czech Republic, belonging to the institution), Daniel PLUSKAL (203 Czech Republic, belonging to the institution), Racha BAATALLAH, Glwadys GAGNOT, José Gaspar RANGEL PAMPLONA PIZARRO PINTO (620 Portugal, belonging to the institution), Vinicius T. T. SANTANA, Markéta STUCHLÁ (203 Czech Republic, belonging to the institution), Petr NEUGEBAUER, Pimchai CHAIYEN, Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution), David BEDNÁŘ (203 Czech Republic, belonging to the institution), Yves L. L. JANIN, Zbyněk PROKOP (203 Czech Republic, belonging to the institution) and Martin MAREK (203 Czech Republic, belonging to the institution)
Edition
Nature Catalysis, Nature Portfolio, 2023, 2520-1158
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10403 Physical chemistry
Country of publisher
Germany
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 37.800 in 2022
RIV identification code
RIV/00216224:14310/23:00130829
Organization unit
Faculty of Science
UT WoS
000906600100001
Keywords in English
CYPRIDINA LUCIFERIN; PROTEIN CRYSTALLIZATION; BIOLUMINESCENCE; RENIFORMIS; LIGHT; CHEMILUMINESCENCE; COELENTERAZINE; STABILITY; LUMINESCENCE; SPECIFICITY
Tags
Tags
International impact, Reviewed
Změněno: 8/4/2024 07:49, Mgr. Marie Šípková, DiS.
Abstract
V originále
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.
Links
EF17_043/0009632, research and development project |
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GA22-09853S, research and development project |
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LM2018121, research and development project |
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LM2018127, research and development project |
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LM2018140, research and development project |
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MUNI/H/1561/2018, interní kód MU |
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792772, interní kód MU |
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814418, interní kód MU |
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857560, interní kód MU (CEP code: EF17_043/0009632) |
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90242, large research infrastructures |
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