Front Cover: Dioxygen Binding Is Controlled by the Protein Environment in Non‐heme FeII and 2‐Oxoglutarate Oxygenases: A Study on Histone Demethylase PHF8 and an Ethylene‐Forming Enzyme (Chem. Eur. J. 24/2023)

The cover shows the oxygen diffusion channel in class 7 histone demethylase (PHF8) and ethylene‐forming enzyme (EFE). PHF8 catalyzes the hydroxylation of its H3 K9me2 histone substrate, and EFE catalyzes two competing reactions of ethylene generation and substrate l‐Arg hydroxylation. Although both...

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Veröffentlicht in:Chemistry : a European journal 2023-04, Vol.29 (24), p.n/a
Hauptverfasser: Chaturvedi, Shobhit S., Thomas, Midhun George, Rifayee, Simahudeen Bathir Jaber Sathik, White, Walter, Wildey, Jon, Warner, Cait, Schofield, Christopher J., Hu, Jian, Hausinger, Robert P., Karabencheva‐Christova, Tatayana G., Christov, Christo Z.
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Sprache:eng
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Zusammenfassung:The cover shows the oxygen diffusion channel in class 7 histone demethylase (PHF8) and ethylene‐forming enzyme (EFE). PHF8 catalyzes the hydroxylation of its H3 K9me2 histone substrate, and EFE catalyzes two competing reactions of ethylene generation and substrate l‐Arg hydroxylation. Although both enzymes initially have an off‐line 2‐oxoglutarate (2OG) conformation, upon oxygen binding, PHF8 forms an in‐line superoxo complex, whereas EFE uses the off‐line superoxo complex. More information can be found in the Research Article by C. Z. Christov and co‐workers. (DOI: 10.1002/chem.202300138).
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.202300853