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Presented By: Department of Chemistry

Understanding structure-function relationships in transition-metal-containing enzymes

Alexey Silakov (The Pennsylvania State University)

The Silakov laboratory seeks to uncover principles underpinning biology\'s control over the reactivity of metal complexes in enzymes. Millions of years of natural selection in harsh, nutrient-limiting environments evolved organisms into highly effective and extremely selective metabolic systems. Organisms from all kingdoms of life are replete with enzymes that facilitate a staggering array of reactions with efficiency using nothing but abundant 3rd-row transition metal ions that is hard to replicate using pure synthetic chemistry approaches. To understand how similar metal-containing catalytic centers can vary their reactivity depending on the protein environment, we employ various advanced experimental methods such as Electron Paramagnetic Resonance and Infrared spectroscopies, (spectro)electrochemistry, and protein film voltammetry. As some knowledge gaps about the function of enzymes stem from the absence of suitable experimental techniques, we also have a strong interested in developing novel biophysical approaches that allow addressing such gaps. This talk will present two case studies performed by the Silakov laboratory: a superfamily of Fe/2OG oxygenases involved in the biosynthesis of natural products, and [FeFe] hydrogenases which are highly effective H2-producing enzymes. The ultimate goal of our fundamental research is to inform the development of new biotechnologies to allow environmentally friendly biosynthetic production of much-needed molecules such as drugs and renewable energy resources.
Alexey Silakov (The Pennsylvania State University)

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