Reducing Agent-Mediated Nonenzymatic Conversion of 2-Oxoglutarate to Succinate: Implications for Oxygenase Assays.
Reducing Agent-Mediated Nonenzymatic Conversion of 2-Oxoglutarate to Succinate: Implications for Oxygenase Assays.
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DOI：
10.1002/cbic.202000185
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发表时间：
2020-10-15
期刊：
影响因子：
--
通讯作者：
Claridge TDW
中科院分区：
文献类型：
--
作者：
Khan A;Schofield CJ;Claridge TDW
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. Taking everything into account: In catalytic reactions by some 2OG oxygenases with prolonged reaction times or high l‐ascorbate concentrations, nonenzymatic reactions of 2‐oxoacids mediated by reactive oxygen species such as H2O2 might be relevant. Knowledge of how catalysis is affected by, say, metal ions or temperature will allow appropriate controls to be implemented in kinetic studies or inhibition assays.
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DOI：
10.1002/chem.201503761
发表时间：
2016-01-22
期刊：
Chemistry (Weinheim an der Bergstrasse, Germany)
影响因子：
--
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DOI：
10.1016/0006-291x(78)91010-0
发表时间：
1978-01-01
影响因子：
3.1
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通讯作者：
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DOI：
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发表时间：
1982-01-01
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
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KEMP, A