biostudies-literatureUnknown9(2)Zhao XCytochrome P450 system consists of P450 monooxygenase and redox pattern(s). While the importance of monooxygenases in plant metabolism is well documented, the metabolic roles of the related redox components have been largely overlooked. Here, we show that distinct electron transfer chains are recruited in phenylpropanoid-monolignol P450 systems to support the synthesis and distribution of different classes of phenolics in different plant tissues. While <i>Arabidopsis</i> cinnamate 4-hydroxylase adopts conventional NADPH-cytochrome P450 oxidoreductase (CPR) electron transfer chain for its <i>para</i>-hydroxylation reaction, ferulate 5-hydroxylase uses both NADPH-CPR-cytochrome <i>b₅</i> (CB5) and NADH-cytochrome <i>b₅</i> reductase-CB5 chains to support benzene ring 5-Science advanceseade4389https://www.ebi.ac.uk/biostudies/studies/S-EPMC9833660biostudies-literatureTissue-preferential recruitment of electron transfer chains for cytochrome P450-catalyzed phenolic biosynthesis.PMC9833660Liu CJGou MZhao YZhao XfalseTissue-preferential recruitment of electron transfer chains for cytochrome P450-catalyzed phenolic biosynthesis.Cytochrome P450 system consists of P450 monooxygenase and redox pattern(s). While the importance of monooxygenases in plant metabolism is well documented, the metabolic roles of the related redox components have been largely overlooked. Here, we show that distinct electron transfer chains are recruited in phenylpropanoid-monolignol P450 systems to support the synthesis and distribution of different classes of phenolics in different plant tissues. While <i>Arabidopsis</i> cinnamate 4-hydroxylase adopts conventional NADPH-cytochrome P450 oxidoreductase (CPR) electron transfer chain for its <i>para</i>-hydroxylation reaction, ferulate 5-hydroxylase uses both NADPH-CPR-cytochrome <i>b₅</i> (CB5) and NADH-cytochrome <i>b₅</i> reductase-CB5 chains to support benzene ring 5-2023-01-01T00:00:00Z2023 Jan2025-04-26T09:50:19.649Z2025-02-18T23:26:00.315ZS-EPMC98336603663049410.1126/sciadv.ade4389