Studies on Luciferase from Photobacterium phosphoreum
- 1 June 1974
- journal article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 75 (6) , 1249-1255
- https://doi.org/10.1093/oxfordjournals.jbchem.a130508
Abstract
The stoichiometry of the reaction of stripped luciferase from Photobacterium phosphoreum was determined to be luciferase: FMNH2: O2=l : 1 : 1. A red shift of FMNH2 absorption bands and quenching of protein fluorescence were observed on binding of FMNH2 to luciferase. The inhibitory effects of FMNH2 derivatives on the luciferase reaction suggested that the isoalloxazine nucleus, ribitol moiety and phosphate group are all involved in the binding of FMNH2 to luciferase. The dissociation constant of the luciferase-FMNH2 complex, estimated by various titrimetric measurements, was 1-6×lO-7M. The affinity of FMN to luciferase was less than 10-5-fold that of FMNH2. The standard potential of luciferase-bound FMN FMNH2 was calculated to be -0.06 V.Keywords
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