Tissue-preferential recruitment of electron transfer chains for cytochrome P450-catalyzed phenolic biosynthesis

• DOI: 10.1126/sciadv.ade4389
• Publication Date: 2023-01-11T18:58:52Z
• Authors: Xianhai Zhao; Yunjun Zhao; Mingyue Gou; Chang-Jun Liu
• Keywords: Hydroxylation; Monolignol; Cytochrome b5; Cytochrome P450 reductase

Cytochrome P450 system consists of monooxygenase and redox pattern(s). While the importance monooxygenases in plant metabolism is well documented, metabolic roles related components have been largely overlooked. Here, we show that distinct electron transfer chains are recruited phenylpropanoid-monolignol systems to support synthesis distribution different classes phenolics tissues. Arabidopsis cinnamate 4-hydroxylase adopts conventional NADPH-cytochrome oxidoreductase (CPR) chain for its para-hydroxylation reaction, ferulate 5-hydroxylase uses both NADPH-CPR-cytochrome b5 (CB5) NADH-cytochrome reductase-CB5 benzene ring 5-hydroxylation, which former route primarily stem syringyl lignin synthesis, while latter dominates syntheses 5-hydroxylated seeds seed coat suberin. Our study unveils an additional layer complexity versatility plants evolved diversifying phenolic repertoires.