Stephen Bell

@bellp450enzyme.bsky.social

Chemist, heme enzyme enthusiast, cytochrome P450 tinkerer.

Surprised and delighted to have been awared this. Thanks to @acs.org Catalysis. Special thanks to those who contributed to the paper Adelaide University especially Matthew Podgorski who lead the experimental work. doi.org/10.1021/acsc... axial.acs.org/organic-chem...

ACS Catalysis 2026 Lectureship and Award Winners | ACS Publications Chemistry Blog

Learn more about the winners of the 2026 ACS Catalysis Lectureship for the Advancement of Catalytic Science.

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Scalable and Stereoselective C–H Bond #Hydroxylation of Steroids Using a Designer #Heme-Thiolate #Peroxygenase Biocatalyst | The Journal of Organic Chemistry pubs.acs.org/doi/10.1021/...

Scalable and Stereoselective C–H Bond Hydroxylation of Steroids Using a Designer Heme-Thiolate Peroxygenase Biocatalyst

A challenging yet critical reaction in chemical synthesis is the selective activation of unactivated carbon–hydrogen bonds in complex molecules. Here we demonstrate the biocatalytic regio- and stereoselective hydroxylation of steroids, including progesterone, testosterone, adrenosterone, androstenedione, and dehydroepiandrosterone (DHEA), using a variant of an engineered bacterial cytochrome P450 enzyme, CYP154C35 from Nocardia otitidiscaviarum. We replaced two amino acid residues within the oxygen-binding groove of the I-helix, and this modification of the acid-alcohol pair to a glutamine and a glutamate set of residues had the effect of converting the enzyme into an efficient peroxygenase (CYP154C35QE). This enzyme performed the biocatalytic oxidation of the steroids stereoselectively to form the 16α-hydroxylated metabolites. In the presence of a substrate, CYP154C35QE was stable to relatively high concentrations of H2O2 but could function catalytically using lower concentrations. The enzyme tolerated 20% DMSO and was not denatured upon being preheated for 1 h at 40 °C. The enzyme was capable of high turnover numbers (∼6500), resulting in complete conversion of the substrate, enabling the formation, purification, and characterization of the enantiopure 16α-hydroxylated steroids at up to 120 mg scale.

pubs.acs.org

A really engaging TIBS Spotlight article highlighting our recent structures of a cytochrome P450 SyoA. Thanks to Professor Jennifer DuBois for elegantly contextualising the work within the broader field of lignin valorisation. Upcycling lignin with a controlled burn tinyurl.com/2s3w9ej6 🔥🫰

Upcycling lignin with a controlled burn

A recent report by Harlington et al. introduces SyoA, a cytochrome P450 enzyme that efficiently removes a methyl group from the S-subunits of lignin. Lignin is one of the most abundant forms of renewa...

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