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Light-Driven Oxidative Demethylation Reaction Catalyzed by a Rieske-Type Non-heme Iron Enzyme Stc2

Weiyao Hu, Kelin Li, Andrew C. Weitz, Aiwen Wen, Hyomin Kim, Jessica C. Murray, Ronghai Cheng, Baixiong Chen, Nathchar Naowarojna, Mark W. Grinstaff, Sean J. Elliott, Jie‐Sheng Chen, Pinghua Liu

2022ACS Catalysis16 citationsDOIOpen Access PDF

Abstract

Rieske-type non-heme iron oxygenases/oxidases catalyze a wide range of transformations. Their applications in bioremediation or biocatalysis face two key barriers: the need of expensive NAD(P)H as a reductant and a proper reductase to mediate the electron transfer from NAD(P)H to the oxygenases. To bypass the need of both the reductase and NAD(P)H, using Rieske-type oxygenase (Stc2) catalyzed oxidative demethylation as the model system, we report Stc2 photocatalysis using eosin Y/sulfite as the photosensitizer/sacrificial reagent pair. In a flow-chemistry setting to separate the photo-reduction half-reaction and oxidation half-reaction, Stc2 photo-biocatalysis outperforms the Stc2-NAD(P)H-reductase (GbcB) system. In addition, in a few other selected Rieske enzymes (NdmA, CntA, and GbcA), and a flavin-dependent enzyme (iodotyrosine deiodinase, IYD), the eosin Y/sodium sulfite photo-reduction pair could also serve as the NAD(P)H-reductase surrogate to support catalysis, which implies the potential applicability of this photo-reduction system to other redox enzymes.

Topics & Concepts

BiocatalysisChemistryNAD+ kinaseReductaseDemethylationRedoxAlcohol dehydrogenaseFlavin groupOxidoreductaseSulfiteCatalysisShewanella oneidensisPhotochemistryCombinatorial chemistryEnzymeBiochemistryOrganic chemistryReaction mechanismBiologyGeneGeneticsBacteriaDNA methylationGene expressionMetal-Catalyzed Oxygenation MechanismsMicrobial Fuel Cells and BioremediationMetalloenzymes and iron-sulfur proteins
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