the luciferase catalyzes the oxidation of luciferin to produce the light emitter after thermolysis of the peroxide intermediate. The light is produced via an ATP-dependent luciferin-luciferase reaction involving oxygen molecule and Mg2+. The oxygenation reaction occurs with a single electron-transfer (SET) mechanism. The luciferin of Watasenia scintillans is a disulfonate derivative of coelenterazine, i.e. coelenterazine disulfonate. Bioluminescence and luciferin oxygenation reaction mechanism, analysis by density functional theory (DFT) and time-dependent DFT (TDDFT), calculation, modeling, and dynamics simulation, detailed overview
light emitter is the excited state of the anion form of coelerenterazine disulfate, quantum yield is calculated at 0.36. the reaction mechanism does not involve formation of a adenyl luciferin intermediate
coelenterazine disulfate is the Watasenia scintillans luciferin substrate, and the reaction requires ATP, Mg2+ and molecular oxygen. Protein microcrystals in the arm photophores catalyse the bioluminescent reaction using ATP and the substrate coelenterazine disulfate
coelenterazine disulfate is the Watasenia scintillans luciferin substrate, and the reaction requires ATP, Mg2+ and molecular oxygen. Protein microcrystals in the arm photophores catalyse the bioluminescent reaction using ATP and the substrate coelenterazine disulfate
photophores at the tips of two arms, the photophores are densely packed with protein microcrystals that catalyse the bioluminescent reaction using ATP and the substrate coelenterazine disulfate
the organism produces flashes of blue light via a series of complicated luciferin-luciferase reactions involving ATP, Mg2+, and molecular oxygen. The enzyme catalyzes the two key steps. They are the addition of molecular oxygen to luciferin and the formation of light emitter. The oxygenation reaction occurs with a single electron-transfer (SET) mechanism, and the light emitter is produced via the mechanism of gradually reversible charge-transfer-induced luminescence (GRCTIL). Biolumiscence key steps are oxygenation of luciferin and thermolysis of the peroxide intermediate to produce light emitter
protein microcrystals in the arm photophores catalyse the bioluminescent reaction using ATP and the substrate coelenterazine disulfate. The crystals contain a major 63 kDa protein and a minor 81 kDa protein, in a mass ratio of about 8 to 1. Three homologous proteins comprise the luminescent arm tip microcrystals, i.e. proteins wsluc1-3, wsluc1-3 form a complex that crystallises inside the squid photophores. Analysis of the proteins from the protein crystal extraction identified by MALDI TOF/TOF mass spectrometry analysis, overview
proteins wsluc1-3 belong to the ANL superfamily. ANL superfamily enzymes have independently evolved in distant species to produce light using unrelated substrates
Watasenia scintillans coelenterazine disulfonate has an imidazopyrazinone skeleton. Besides the firefly and bacteria bioluminescence, the bioluminescence coming from imidazopyrazinone derivatives-based luciferin or luminescent substrate of photoprotein is the most known one, which covers eight phyla, i.e. radiolaria, cnidaria, chordata, ctenophora, mollusca, arthropoda, echinodermata, and chaetognatha. The oxygenation process is not only crucial to Watasenia scintillans bioluminescence, but also a general step in almost all oxygen-dependent bioluminescence systems, such as firefly, sea firefly, jellyfish, Obelia, and bacteria
mutation changes the enzymatic decay rate by inducing a substantial tertiary structural change, without a large effect on secondary structural elements
three proteins termed wsluc1 (encoded by transcript 82699_c0_seq1), wsluc2 (81000_c2_seq2) and wsluc3 (83251_c0_seq1), sequence comparisons and phylogenetic analysis, transcriptome analysis