Firefly luciferase produces hydrogen peroxide as a coproduct in dehydroluciferyl adenylate formation

• Type: Article in International Scientific Journal
• Date: 2006

Authors

Fraga, H (Author) Other; Fernandes, D (Author) Other; Novotny, J (Author) Other; Fontes, R (Author) FMUP; da Silva, JCG (Author) FCUP

Journal

Title: ChemBioChem

Vol. 7

Pages: 929-935

ISSN: 1439-4227

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 48 Citations

Scopus - 51 Citations

Scientific classification

FOS: Medical and Health sciences > Basic medicine

Other information

Authenticus ID: P-004-KAT

DOI: 10.1002/cbic.200500443

Abstract (EN): Firefly luciferase catalyzes the synthesis of H2O2 from the same substrates as the bioluminescence reaction: ATP and luciferin (D-LH2). About 80% of the enzyme-bound intermediate D-luciferyl adenylate (D-LH2-AMP) is oxidized into oxyluciferin, and a photon is emitted during this reaction. The enzyme pathway responsible for the generation of H2O2 is a side reaction in which D-LH2-AMP is oxidized into dehydroluciferyl adenylate (L-AMP). Like the bioluminescence reaction, the luciferase-catalyzed synthesis of H2O2 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7