Biocatalyst Engineering

Our group has had a longstanding interest in expanding the utility of enzymes as practical catalysts, especially for synthetically useful reactions in nonaqueous media and biotransformations under unnatural conditions. Examples of recent achievements in this area include engineering cytochrome P450s to utilize biomimetic cofactors, developing self-renaturing enzymes, establishing a high-temperature benchmark for biocatalysis, and constructing highly stable protein arrays and microfluidic reactors based on sol-gel immobilized enzymes.

Building upon our earlier use of salt-activation and ion-paired solubilization, two groundbreaking methods for greatly increasing enzyme activities in nonaqueous environments, we have been using advanced spectroscopic techniques (e.g., EPR and multinuclear NMR methods) to study protein structure and dynamics as a function of solvent properties and protein hydration, thus elucidating structure-function relationships for enzymes across a broad spectrum of environments.

Most recently, we have collaborated with the Hartwig Group to create and evolve artificial metalloenzymes capable of catalyzing synthetically-important, abiological reactions.

 

A surfactant solubilized enzyme in an organic solvent

 

NMR visible active-site probe

 

An immobilized enzyme-chaperone chimera