Sam Hay

This paper introduces multistate enzyme design to optimize active sites across reaction coordinates, achieving higher catalytic efficiency and enantioselectivity than single-state designs.

The paper describes the photoactivation mechanism of the B12 photoreceptor CarH using structural and spectroscopic methods, revealing unique intermediates that drive tetramer dissociation.

The paper develops a bioinformatics workflow to identify diverse cellulose-binding domains through in silico prioritisation and high-throughput screening, identifying 5 CBMs with significant binding to cellulose materials.

The paper investigates structural models of the POR-Pchlide-NADPH ternary complex and proposes an alternative model based on mutagenesis and computational analysis, identifying key residues involved in catalysis.

The paper uses time-resolved infrared spectroscopy to study electron density flow in coenzyme B12 of CarH, showing how the protein avoids radical photoproducts during its photoresponse.