Assembly of a Rieske non-heme iron oxygenase multicomponent system from Phenylobacterium immobile E DSM 1986 enables pyrazon cis-dihydroxylation in E. coli

• DOI: 10.1007/s00253-021-11129-w
• Publication Date: 2021-02-14T13:42:49Z
• Authors: Andreas Hunold; Wendy Escobedo-Hi...; Elsa Potoudis; Daniela Resende; Theresa Farr; Per-Olof Syrén; Bernhard Hauer
• Keywords: Dihydroxylation; Multicopper oxidase; Dioxygenase

Abstract Phenylobacterium immobile strain E is a soil bacterium with striking metabolism relying on xenobiotics, such as the herbicide pyrazon, sole carbon source instead of more bioavailable molecules. Pyrazon heterocyclic aromatic compound environmental concern and its biodegradation pathway has only been reported in P. . The multicomponent pyrazon oxygenase (PPO), Rieske non-heme iron oxygenase, incorporates molecular oxygen at 2,3 position phenyl moiety first step degradation, generating cis -dihydrodiendiol. aim this work was to identify genes encoding for each one PPO components enable their functional assembly Escherichia coli genome sequencing revealed RO components, ferredoxin-, reductase-, α- β-subunits an oxygenase. Though, displays three prominent differences respect ROs currently characterized: (1) operon-like organization absent, (2) all elements are randomly scattered DNA, (3) not one, but 19 different α-subunits encoded genome. Herein, we report identification involved -dihydroxylation immobile, appropriate assembly, reconstitution E. Our results contributes essential missing pieces complete overall elucidation from Key points • DSM 1986 harbors described (PPO). We elucidated components. Heterologous expression enabled dihydroxylation JW5510.