Rational Design of Artificial Hydrogenases

Friday, February 28, 2020


Dr. Saumen Chakraborty

Department of Chemistry and Biochemistry

The University of Mississippi

Reception: Hand 1130 at 3:00 PM

Seminar: Hand 1144 at 3:30 PM

Abstract: Metalloenzymes carry out difficult transformations in nature with unprecedented efficiency. Hydrogenases are a group of complex metalloenzymes that provide energy for certain organisms by facile interconversion between protons and hydrogen gas in an efficient and reversible manner. Understanding the structure-function relationships of hydrogenases would facilitate hydrogenase-inspired biocatalyst development. However, the complexity of the enzyme due to the presence of multiple metallic cofactors and O2 intolerance makes realizing these dreams challenging. One avenue to circumvent this problem is via developing “artificial hydrogenases”. Among others, metalloprotein reengineering is an attractive approach that allows for rational design of artificial metalloenzymes within simplified and robust constructs. Inspired by this approach, recent developments in redesigning a copper protein into a nickel binding protein as a functional model of hydrogenases and related de novo designed protein systems in my laboratory will be described. Approaches to incorporate unnatural amino acids and to assemble the binuclear active sites within these artificial hydrogenases in order to enhance the reactivity, reversibility and sustainability will be discussed

Bio: Saumen Chakraborty is an Assistant Professor at the Chemistry and Biochemistry Department of the University of Mississippi. He earned his Ph.D. in chemistry from the University of Michigan under the guidance of Prof. Vincent Pecoraro in de novo protein design. He received postdoctoral trainings at the University of Illinois in the laboratory of Prof. Yi Lu in metalloprotein design and at the Los Alamos National Laboratory with Dr. Jennifer Martinez in bionanomaterials for energy applications. His research interests are bioinorganic chemistry and alternate energy research.


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