title: Bioluminescence of the arm light organs of the luminous squid Watasenia scintillans.
abstract: The squid Watasenia scintillans emits blue light from numerous photophores. According to Tsuji [F.I. Tsuji, Bioluminescence reaction catalyzed by membrane-bound luciferase in the "firefly squid", Watasenia scintillans, Biochim. Biophys. Acta 1564 (2002) 189-197.], the luminescence from arm light organs is caused by an ATP-dependent reaction involving Mg2+, coelenterazine disulfate (luciferin), and an unstable membrane-bound luciferase. We stabilized and partially purified the luciferase in the presence of high concentrations of sucrose, and obtained it as particulates (average size 0.6-2 microm). The ATP-dependent luminescence reaction of coelenterazine disulfate catalyzed by the particulate luciferase was investigated in detail. Optimum temperature of the luminescence reaction is about 5 degrees C. Coelenterazine disulfate is a strictly specific substrate in this luminescence system; any modification of its structure resulted in a very heavy loss in its light emission capability. The light emitter is the excited state of the amide anion form of coelenteramide disulfate. The quantum yield of coelenterazine disulfate is calculated at 0.36. ATP could be replaced by ATP-gamma-S, but not by any other analogues tested. The amount of AMP produced in the luminescence reaction was much smaller than that of coelenteramide disulfate, suggesting that the reaction mechanism of the Watasenia bioluminescence does not involve the formation of adenyl luciferin as an intermediate.
authors.affiliation: Faculty of Bioresources, Mie University, Tsu, Mie 514-8507, Japan. teranisi@bio.mie-u.ac.jp
authors.forename: Katsunori
authors.initials: K
authors.lastname: Teranishi
authors.forename: Osamu
authors.initials: O
authors.lastname: Shimomura
mesh_terms: D000244:Adenosine Diphosphate / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000737:chemistry; D000825:Animal Structures / Q000737:chemistry / Q000201:enzymology; D000818:Animals; D002384:Catalysis; D049832:Decapodiformes / Q000737:chemistry / Q000201:enzymology*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles / Q000737:chemistry; D007700:Kinetics; D008156:Luciferases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D049449:Luminescence; D008163:Luminescent Measurements; D015636:Magnesium Chloride / Q000737:chemistry; D015394:Molecular Structure; D010316:Particle Size; D010777:Photochemistry; D011719:Pyrazines / Q000737:chemistry; D013053:Spectrophotometry; D013347:Subcellular Fractions / Q000737:chemistry / Q000201:enzymology; D013395:Sucrose / Q000737:chemistry; D013696:Temperature
chemical_list: D007093:Imidazoles; D011719:Pyrazines; D015636:Magnesium Chloride; C017144:coelenterazine; D013395:Sucrose; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D008156:Luciferases