Literature summary for 1.13.12.24 extracted from

Hori, K.; Anderson, J.; Ward, W.; Cormier, M.
Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence, assignment of luciferin tautomers in aequorin and mnemiopsin (1975), Biochemistry, 14, 2371-2376 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	the binding of calcium ion to the photoprotein brings about a conformational change in the protein which results in the chromophore reacting with a protein side chain hydroperoxide to yield a protein bound luciferin hydroperoxide intermediate. This intermediate then decomposes to CO2 and an electronic excited state of the corresponding protein-oxyluciferin monoanion complex which leads to light emission	Aequorea victoria

Organism

Organism	UniProt	Comment	Textmining
Aequorea victoria	P02592	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	aequorin exhibits an absorption near 454 nm. The native chromophore is Renilla luciferin or a nearly identical derivative. The binding of calcium ion to the photoprotein brings about a conformational change in the protein which results in the chromophore reacting with a protein side chain hydroperoxide to yield a protein bound luciferin hydroperoxide intermediate. This intermediate then decomposes to CO2 and an electronic excited state of the corresponding protein-oxyluciferin monoanion complex which leads to light emission	Aequorea victoria	?	-	?

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Release 2023.1 (January 2023)