Artificial Metalloenzymes

This research pillar combines synthetic Ir(III) and Zn(II) porphyrins with engineered cytochrome b₅₆₂ variants to investigate how a protein environment can shape non-natural cofactor binding and reactivity. My independent [synthetic organic chemistry portfolio](/synthetic-chemistry/) covers compound libraries, coumarins, diazirines, porphyrins and BODIPY analogues.

2022–2026PhD Chemistry · University of Cambridge

2021–2022MSc Chemistry · Rhodes University

2020BSc Honours Chemistry · Rhodes University

Artificial metalloenzymes

Synthetic porphyrin–protein conjugates

My PhD at the University of Cambridge explores engineered cytochrome b₅₆₂ variants as scaffolds for synthetic metalloporphyrins. The work asks how a protein environment can be redesigned to give non-natural metal cofactors enzyme-like selectivity and function.

Why artificial metalloenzymes? They seek to combine the broad, non-natural reactivity of organometallic complexes with the selectivity and mild operating conditions of enzymes.

CofactorsIr(III) and Zn(II) metalloporphyrins

Protein platformEngineered cytochrome b₅₆₂ variants

MethodsUV–Vis, fluorescence, NMR, HPLC, HRMS and IR

My contributions include:

• designing and synthesising synthetic metalloporphyrin cofactors;
• optimising metalation and functionalisation reactions;
• engineering and producing protein variants for selective cofactor binding;
• establishing quantitative cofactor-binding assay workflows;
• interpreting structure–function relationships across protein and porphyrin panels; and
• investigating preliminary carbene-transfer chemistry, including cyclopropanation.

Cofactor assembly. A synthetic metalloporphyrin is introduced into the engineered protein scaffold to create a defined, tunable cofactor environment.

Analytical method development

I established new analytical workflows as research questions demanded them. These included UV–visible and fluorescence titrations for protein–cofactor binding, chromatography for purity assessment, NMR and HRMS for molecular characterisation, and singlet-oxygen quantum-yield measurements for photoactive compounds.

This experience has made me comfortable moving between routine, reproducible analysis and open-ended troubleshooting when a method or reaction does not behave as expected.

Future direction: global health

My long-term direction is medicinal chemistry and drug discovery for malaria and other infectious diseases. I am particularly interested in the full path from molecular hypothesis to useful therapeutic: target selection, compound design, structure–activity relationships, synthesis, biological evaluation and developability.

I want to apply rigorous chemistry to health challenges where scientific progress can translate into profound human impact.