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Aequorea victoria is a type of jellyfish that is known by its famous protein,green fluorescent protein(GFP),which has been widely used as a probe in many fields.Aequorea has another important protein,aequorin,which is one of the members of the EF-hand calcium-binding protein family.Aequorin has been used for intracellular calcium measurements for three decades,but its bioluminescence mechanism remains largely unknown.One of the important reasons is the lack of clear and reliable knowledge about the light emitters,which are complex.Several neutral and anionic forms exist in chemiexcited,bioluminescent and fluorescent states and are connected with the H-bond network of the binding cavity in the protein.We theoretically investigated aequorin chemiluminescence,bioluminescence and fluorescence of coelenteramide in vacumm,solvent and real proteins by performing hybrid quantum mechanics and molecular mechanics methods combined with a molecular dynamics method.For the first time,this study reported the origin and clear differences in the chemiluminescence,bioluminescence and fluorescence of coelenteramide,which is important for understanding the bioluminescence not only of jellyfish but also of many other marine organisms(that have the same coelenterazine caved in different coelenterazine-type luciferases).