Abstract
l‐Ascorbate (l‐Asc) is often added to assays with isolated FeII‐ 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.
Highlights
Figure S2. 1H NMR time course analysis of L-Asc mediated 2OG conversion to succinate. (a) Overlay of 1H NMR spectra of an L-Asc/2OG/Tris-D11 buffer mixture for the shown times. (b) Plot showing L-Asc degradation and simultaneous 2OG reaction to give succinate over time
Error bars represent standard deviations from the mean (n =3) of three separate measurements
Summary
Figure S2. 1H NMR time course analysis of L-Asc mediated 2OG conversion to succinate. (a) Overlay of 1H NMR spectra (partial spectra are shown for clarity) of an L-Asc/2OG/Tris-D11 buffer mixture for the shown times. (b) Plot showing L-Asc degradation and simultaneous 2OG reaction to give succinate over time.
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