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J. Biochem, 1977, Vol. 81, No. 4 1057-1062
© 1977 Japanese Biochemical Society

research-article

Studies on Luciferase from Photobacterium phosphoreum

IX. Further Studies on the Spectroscopic Characteristics of the Enzyme-FMN Intermediates1

Naoki ASHIZAWA, Takao NAKAMURA and Takahide WATANABE

Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560

The absorption and fluorometric changes of the reaction mixture of luciferase-FMNH2 complex with O2 were re-examined. Rapid formation (k2(a p p) =2.0 s–1 at [O2]= 120µM) of an intermediate with a single absorption maximum at 380 nm within the range of 350–550 nm, and a weak fluorescence at 520 nm (≤10% of that of FMN when excited at 380 nm) was observed. The absorption and fluorescence spectra and decay rate of the intermediate were estimated by simulation using an analog computer. The decay rate (0.27 s–1 at 20°C) was in agreement with that of an obligatory intermediate of the luminescent reaction previously determined by measuring aldehyde-initiated luminescence. The process of decay of X1 to FMN involved another intermediate X1' with spectroscopic characteristics rather similar to those of FMN.

1This work was supported in part by a grant (No.158036) from the Ministry of Education, Science and Culture of Japan.


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