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Firefly Luciferase Produces Hydrogen Peroxide as a Coproduct in Dehydroluciferyl Adenylate Formation
Author(s) -
Fraga Hugo,
Fernandes Diogo,
Novotny Jiri,
Fontes Rui,
Esteves da Silva Joaquim C. G.
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500443
Subject(s) - luciferase , bioluminescence , adenylate kinase , chemistry , luciferin , stereospecificity , hydrogen peroxide , stereochemistry , enzyme , photochemistry , luciferases , enantiomeric excess , catalysis , biochemistry , enantioselective synthesis , transfection , gene
Firefly luciferase catalyzes the synthesis of H 2 O 2 from the same substrates as the bioluminescence reaction: ATP and luciferin ( d‐ LH 2 ). About 80 % of the enzyme‐bound intermediate d‐ luciferyl adenylate ( d‐ LH 2 ‐AMP) is oxidized into oxyluciferin, and a photon is emitted during this reaction. The enzyme pathway responsible for the generation of H 2 O 2 is a side reaction in which d‐ LH 2 ‐AMP is oxidized into dehydroluciferyl adenylate ( L‐AMP ). Like the bioluminescence reaction, the luciferase‐catalyzed synthesis of H 2 O 2 and L‐AMP is a stereospecific process, involving only the natural D enantiomer. However, the intramolecular electron transfer postulated as essential to the light emission process is not involved in this side reaction.