Open AccessStructure of the oxygen adduct intermediate in the bacterial luciferase reaction: 13 C nuclear magnetic resonance determination
Author(s) -
Sandro Ghisla,
J. Woodland Hastings,
Vincent Favaudon,
JeanMarc Lhoste
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.12.5860
Subject(s) - adduct , electrophile , chemistry , luciferase , oxygen , flavin group , resonance (particle physics) , photochemistry , stereochemistry , nuclear magnetic resonance , biochemistry , enzyme , organic chemistry , catalysis , physics , particle physics , transfection , gene
By using FMN enriched in13 C (90%) at position C-4a, we have conclusively shown that the reaction of molecular oxygen with bacterial luciferase-bound FMNH2 forms an adduct at the 4a position. Consistent with this are13 C NMR studies of FMN and other flavin compounds which show that this carbon should be unusually reactive in the reduced 1,5-dihydroflavins with respect to electrophilic attacks.