Results 11 to 20 of about 6,471 (200)

Investigation of the Superoxide Anion-Triggered Chemiluminescence of Coelenterazine Analogs [PDF]

open access: yesApplied Sciences, 2023
Reactive oxygen species (ROS), including superoxide anion, are involved in regulating various signaling pathways and are also responsible for oxidative stress. Sensing superoxide anion is of particular importance due to its biological significance.
El Hadi Erbiai   +3 more
doaj   +2 more sources

Chiral deaza-coelenterazine analogs for probing a substrate-binding site in the Ca2+-binding photoprotein aequorin.

open access: yesPLoS ONE, 2021
The Ca2+-binding photoprotein aequorin is a complex of apoAequorin (apoprotein) and (S)-2-peroxycoelenterazine. Aequorin can be regenerated by the incubation of apoAequorin with coelenterazine and molecular oxygen (O2).
Satoshi Inouye   +5 more
doaj   +2 more sources

Evidence for de novo Biosynthesis of the Luminous Substrate Coelenterazine in Ctenophores

open access: yesiScience, 2020
Summary: Coelenterazine is a key substrate involved in marine bioluminescence which is used for light-production by at least nine phyla. Some luminous animals, such as the hydromedusa Aequorea, lack the ability to produce coelenterazine endogenously and ...
Manabu Bessho-Uehara   +5 more
doaj   +2 more sources

Coelenterazine sulfotransferase from Renilla muelleri.

open access: yesPLoS ONE, 2022
The luciferin sulfokinase (coelenterazine sulfotransferase) of Renilla was previously reported to activate the storage form, luciferyl sulfate (coelenterazine sulfate) to luciferin (coelenterazine), the substrate for the luciferase bioluminescence ...
George Tzertzinis   +7 more
doaj   +3 more sources

Occurrence of Isopenicillin-N-Synthase Homologs in Bioluminescent Ctenophores and Implications for Coelenterazine Biosynthesis. [PDF]

open access: yesPLoS ONE, 2015
The biosynthesis of the luciferin coelenterazine has remained a mystery for decades. While not all organisms that use coelenterazine appear to make it themselves, it is thought that ctenophores are a likely producer.
Warren R Francis   +4 more
doaj   +2 more sources

Development of a Coelenterazine Derivative with Enhanced Superoxide Anion-Triggered Chemiluminescence in Aqueous Solution [PDF]

open access: yesChemosensors, 2022
Superoxide anion is a reactive oxygen species (ROS) of biological interest. More specifically, it plays a role in intra- and intercellular signaling, besides being associated with conditions such as inflammation and cancer.
José Pedro Silva   +3 more
doaj   +2 more sources

Oxygen Activation of Apo‐obelin–Coelenterazine Complex

open access: yesChemBioChem, 2013
AbstractCa2+‐regulated photoproteins use a noncovalently bound 2‐hydroperoxycoelenterazine ligand to emit light in response to Ca2+ binding. To better understand the mechanism of formation of active photoprotein from apoprotein, coelenterazine and molecular oxygen, we investigated the spectral properties of the anaerobic apo‐obelin–coelenterazine ...
Eremeeva, E.   +6 more
openaire   +4 more sources

The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores [PDF]

open access: yesScientific Reports
Isoforms of some ctenophore photoproteins show different maxima of bioluminescence spectra— the ones of mnemiopsin and bolinopsin have λmax at 490 and 500 nm, while λmax for velamin isoforms are at 500 and 508 nm.
Ludmila P. Burakova, Eugene S. Vysotski
doaj   +2 more sources

A coelenterazine-type bioluminescent probe for nitroreductase imaging

open access: yesOrganic & Biomolecular Chemistry, 2018
Novel coelenterazine-type bioluminescent probes have been designed and synthesized to detect nitroreductase (NTR) in hypoxic tumors.
Xingye Yang   +4 more
openaire   +3 more sources

Mutational optimization of the coelenterazine-dependent luciferase from Renilla [PDF]

open access: yesPlant Methods, 2008
Renilla luciferase (RLUC) is a popular reporter enzyme for gene expression and biosensor applications, but it is an unstable enzyme whose catalytic mechanism remains to be elucidated.
Woo Jongchan, von Arnim Albrecht G
doaj   +3 more sources

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