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

ABSTRACT: 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 Arabidopsis cinnamate 4-hydroxylase adopts conventional NADPH-cytochrome P450 oxidoreductase (CPR) electron transfer chain for its para-hydroxylation reaction, ferulate 5-hydroxylase uses both NADPH-CPR-cytochrome b₅ (CB5) and NADH-cytochrome b₅ reductase-CB5 chains to support benzene ring 5-

SUBMITTER: Zhao X 

PROVIDER: S-EPMC9833660 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature