Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Oxygen detoxification by dienoyl-CoA oxidase involving flavin/disulfide cofactors


Scheffen,  Marieke
Max Planck Institute for Terrestrial Microbiology_others, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

External Resource

(Publisher version)

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Schmid, G., Scheffen, M., Willistein, M., & Boll, M. (2020). Oxygen detoxification by dienoyl-CoA oxidase involving flavin/disulfide cofactors. Molecular Microbiology, 114(1), 17-30. doi:10.1111/mmi.14493.

Cite as: https://hdl.handle.net/21.11116/0000-000E-0BDA-1
Abstract Class I benzoyl-CoA reductases (BCRs) are oxygen-sensitive key enzymes in the degradation of monocyclic aromatic compounds in anaerobic prokaryotes. They catalyze the ATP-dependent reductive dearomatization of their substrate to cyclohexa-1,5-diene-1-carboxyl-CoA (1,5-dienoyl-CoA). An aromatizing 1,5-dienoyl-CoA oxidase (DCO) activity has been proposed to protect BCRs from oxidative damage, however, the gene and its product involved have not been identified, yet. Here, we heterologously produced a DCO from the hyperthermophilic euryarchaeon Ferroglobus placidus that coupled the oxidation of two 1,5-dienoyl-CoA to benzoyl-CoA to the reduction of O2 to water at 80°C. DCO showed similarities to members of the old yellow enzyme family and contained FMN, FAD and an FeS cluster as cofactors. The O2-dependent activation of inactive, reduced DCO is assigned to a redox thiol switch at Eo? = ?3 mV. We propose a catalytic cycle in which the active site FMN/disulfide redox centers are reduced by two 1,5-dienoyl-CoA (reductive half-cycle), followed by two consecutive two-electron transfer steps to molecular oxygen via peroxy- and hydroxyflavin intermediates yielding water (oxidative half-cycle). This work identified the enzyme involved in a unique oxygen detoxification process for an oxygen-sensitive catabolic enzyme.