PMID: 2502778May 1, 1989Paper

The peroxidase/oxidase activity of soybean lipoxygenase--I. Triplet excited carbonyls from the reaction with isobutanal and the effect of glutathione

Photochemistry and Photobiology
T Schulte-Herbrüggen, H Sies

Abstract

Soybean lipoxygenase shows a secondary peroxidase/oxidase activity: The aerobic reaction with isobutanal, enhanced by hydrogen peroxide as a cosubstrate, yields acetone, exhibits chemiluminescence and consumes oxygen (phi cl = 1.3 x 10(-9) photons/O2 molecule consumed). 9,10-Dibromoanthracene-2-sulfonate increases the photoemission (kET tau 0 = 2 x 10(4) M-1; phi cl = 0.9 x 10(-7) photons/O2), whereas it is diminished by sorbate, tryptophan, 2-methyl-1,4-naphthoquinone, glutathione, and superoxide dismutase. In the presence of hydrogen peroxide the lipoxygenase reaction with glutathione yields yet another excited state. From the well-known reactions promoted by horseradish-peroxidase, these features are concluded to indicate the novel activity of soybean lipoxygenase. With isobutanal as a substrate lipoxygenase acts as an oxidase and as a peroxidase. The mechanism suggested leads to photoemissive triplet excited acetone as expected from the cleavage of an intermediate dioxetane.

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Citations

Apr 1, 1995·Journal of Biochemical Toxicology·P RoyA P Kulkarni
Jul 1, 1995·Free Radical Biology & Medicine·G Cilento, W Adam
Jan 4, 1994·Proceedings of the National Academy of Sciences of the United States of America·F D KnudsenG Cilento
Jul 21, 2012·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Sayuri MiyamotoPaolo Di Mascio
May 13, 2018·Trends in Molecular Medicine·Douglas E BrashUNKNOWN Excited-State Medicine Working Group

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