Site-selective protein modification with homogeneous transition-metal catalysts by Zachary Ball, Department of Chemistry, Rice University

Event
Friday, November 15, 2019 - 1:10pm
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Zachary BallZachary Ball

Department of Chemistry, Rice University

(VanVeller)

Chemists are fascinated by metalloenzymes and their chemistry. The reactivity and selectivity of enzyme processes would be powerful practical advances if harnessed in designed transition-metal catalysts. But designing enzyme-like catalysts from scratch has proven exceedingly challenging. Substrate selectivity in polyfunctional environments and highly reactive intermediates incompatible with the bulk aqueous media are properties that are typically too complex and challenging to replicate in simplified, designed systems. Our own efforts have taken advantage of diverse concepts, such as molecular recognition, biomimetic assembly, and structure–function relationships to pursue new methods for site-selective chemistry.