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March 19, 2026ACS Catalysis

Design, Optimization and Characterization of a de novo Gold Hydroaminase

Elinor Morris Boris Lozhkin Jan Uhrhan Indrek Kalvet Sophie Basler Roman P. Jakob David B. Baker Prof. Thomas R. Ward

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Key Points

The aim is to design and optimize a gold hydroaminase using a de novo protein scaffold.
Assembly of an artificial metalloenzyme using a gold complex and tandem repeat protein.
Screening variants for catalytic activity in hydroamination reactions.
Structure-guided mutagenesis to enhance enzyme performance.
Biophysical and crystallographic analyses to study cofactor binding and active site structure.
Identified a variant of the enzyme with significantly higher catalytic activity than the free gold cofactor.
Achieved a double mutant with up to 4-fold increased catalytic rates compared to the original design.
Showed that structural changes in the active site correlate with enhanced catalytic performance.
Demonstrated robustness of the enzyme under harsh conditions, unlike the free cofactor which was deactivated.

Implication

Research shows improved catalytic activity of a gold hydroaminase in engineered proteins, suggesting new design principles for robust catalysts.

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Cite This Study

Morris et al. (2026) studied this question.

synapsesocial.com/papers/69be35836e48c4981c673d61 https://doi.org/10.1021/acscatal.5c08100

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