Details

Autor(en) / Beteiligte

• Qi, Feifei
• Zhang, Wei
• Xue, Yingying
• Geng, Ce
• Huang, Xuenian
• Sun, Jia
• Lu, Xuefeng

Titel

Bienzyme-Catalytic and Dioxygenation-Mediated Anthraquinone Ring Opening

Ist Teil von

• Journal of the American Chemical Society, 2021-10, Vol.143 (40), p.16326-16331

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2021

Quelle

MEDLINE

Beschreibungen/Notizen

• The C-10–C-4a bond cleavage of anthraquinone is believed to be a crucial step in fungal seco-anthraquinone biosynthesis and has long been proposed as a classic Baeyer–Villiger oxidation. Nonetheless, genetic, enzymatic, and chemical information on ring opening remains elusive. Here, a revised questin ring-opening mechanism was elucidated by in vivo gene disruption, in vitro enzymatic analysis, and 18O chasing experiments. It has been confirmed that the reductase GedF is responsible for the reduction of the keto group at C-10 in questin to a hydroxyl group with the aid of NADPH. The C-10–C-4a bond of the resultant questin hydroquinone is subsequently cleaved by the atypical cofactor-free dioxygenase GedK, giving rise to desmethylsulochrin. This proposed bienzyme-catalytic and dioxygenation-mediated anthraquinone ring-opening reaction shows universality.