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• W3031759969 abstract "Abstract l ‐Ascorbate ( l ‐Asc) is often added to assays with isolated Fe II ‐ and 2‐oxoglutarate (2OG)‐dependent oxygenases to enhance activity. l ‐Asc is proposed to be important in catalysis by some 2OG oxygenases in vivo . We report observations on the nonenzymatic conversion of 2OG to succinate, which is mediated by hydrogen peroxide generated by the reaction of l ‐Asc and dioxygen. Slow nonenzymatic oxidation of 2OG to succinate occurs with some, but not all, other reducing agents commonly used in 2OG oxygenase assays. We intend these observations will help in the robust assignment of substrates and inhibitors for 2OG oxygenases." @default.
• W3031759969 created "2020-06-05" @default.
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• W3031759969 date "2020-08-18" @default.
• W3031759969 modified "2023-10-13" @default.
• W3031759969 title "Reducing Agent‐Mediated Nonenzymatic Conversion of 2‐Oxoglutarate to Succinate: Implications for Oxygenase Assays" @default.
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• W3031759969 doi "https://doi.org/10.1002/cbic.202000185" @default.
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