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Characterization of O2 uncoupling in biodegradation reactions of nitroaromatic contaminants catalyzed by rieske oxygenases.
Bopp, Charlotte E; Bernet, Nora M; Pati, Sarah G; Hofstetter, Thomas B.
Affiliation
  • Bopp CE; Eawag, Swiss Federal Institute of Aquatic Science and Technology, Dübendorf, Switzerland; Institute of Biogeochemistry and Pollutant Dynamics (IBP), ETH Zürich, Zürich, Switzerland.
  • Bernet NM; Eawag, Swiss Federal Institute of Aquatic Science and Technology, Dübendorf, Switzerland; Institute of Biogeochemistry and Pollutant Dynamics (IBP), ETH Zürich, Zürich, Switzerland.
  • Pati SG; Department of Environmental Geosciences, Centre for Microbiology and Environmental Systems Science, University of Vienna, Vienna, Austria.
  • Hofstetter TB; Eawag, Swiss Federal Institute of Aquatic Science and Technology, Dübendorf, Switzerland; Institute of Biogeochemistry and Pollutant Dynamics (IBP), ETH Zürich, Zürich, Switzerland. Electronic address: thomas.hofstetter@eawag.ch.
Methods Enzymol ; 703: 3-28, 2024.
Article in En | MEDLINE | ID: mdl-39261002
ABSTRACT
Rieske oxygenases are known as catalysts that enable the cleavage of aromatic and aliphatic C-H bonds in structurally diverse biomolecules and recalcitrant organic environmental pollutants through substrate oxygenations and oxidative heteroatom dealkylations. Yet, the unproductive O2 activation, which is concomitant with the release of reactive oxygen species (ROS), is typically not taken into account when characterizing Rieske oxygenase function. Even if considered an undesired side reaction, this O2 uncoupling allows for studying active site perturbations, enzyme mechanisms, and how enzymes evolve as environmental microorganisms adapt their substrates to alternative carbon and energy sources. Here, we report on complementary methods for quantifying O2 uncoupling based on mass balance or kinetic approaches that relate successful oxygenations to total O2 activation and ROS formation. These approaches are exemplified with data for two nitroarene dioxygenases (nitrobenzene and 2-nitrotoluene dioxygenase) which have been shown to mono- and dioxygenate substituted nitroaromatic compounds to substituted nitrobenzylalcohols and catechols, respectively.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxygen / Oxygenases / Biodegradation, Environmental Language: En Journal: Methods Enzymol Year: 2024 Document type: Article Affiliation country: Suiza Country of publication: Estados Unidos

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxygen / Oxygenases / Biodegradation, Environmental Language: En Journal: Methods Enzymol Year: 2024 Document type: Article Affiliation country: Suiza Country of publication: Estados Unidos