Reducing Agent‐Mediated Nonenzymatic Conversion of 2‐Oxoglutarate to Succinate: Implications for Oxygenase Assays

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 med...

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Detalles Bibliográficos
Autores principales: Khan, Amjad, Schofield, Christopher J., Claridge, Timothy D. W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7693218/
https://www.ncbi.nlm.nih.gov/pubmed/32478965
http://dx.doi.org/10.1002/cbic.202000185
Descripción
Sumario: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.

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