Characterisation of the Self-Sufficient Cytochrome P450 CYP116B234 From Rhodococcus globerulus and Its Suggested Native Role in 2-Hydroxyphenylacetic Acid Metabolism.

ABSTRACT: Cytochromes P450 (P450s) are exceptional biocatalysts that enable the selective oxidation of unactivated C-H bonds using molecular oxygen. Typically, auxiliary redox partner proteins deliver electrons from NAD(P)H to the P450, enabling oxygen activation. However, associating native redox partners with P450s can be challenging, particularly when they are genomically separated. Self-sufficient P450s, where the P450 heme domain is naturally fused to redox partners, represent a simpler, single-protein system. Here, we present CYP116B234, a novel self-sufficient P450 from Rhodococcus globerulus, comprising fused heme and phthalate-family oxygenase reductase (PFOR) domains. The gene encoding CYP116B234 was codon-optimised for heterologous expression in E. coli and subsequently purified to homoge

SUBMITTER: Kundral S 

PROVIDER: S-EPMC11889516 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature