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Updated: Oct 2, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Unprecedented overmetabolism of a porphyrinogen substrate by coproporphyrinogen oxidase
Timothy D Lash1, Anna-Sigrid I M Keck, Ukti N Mani
1Department of Chemistry, Illinois State University, Normal, IL 61790-4160, USA. tdlash@ilstu.edu
Abstract:
Harderoporphyrinogen-I is metabolized by avian hemolysate preparations of coproporphyrinogen oxidase to give a trivinylic product; this unprecedented 'overmetabolism' of the porphyrinogen substrate provides strong support for a proposed model of the active site of this poorly understood enzyme.
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