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Biocatalysis

Photo of Squire Booker

Squire Booker - F1000 Faculty Member (since 29 May 2008)

Department of Biochemistry & Molecular Biology, The Pennsylvania State University, University Park, PA, USA

BIOGRAPHY

ACADEMIC POSITIONS:
• Associate Professor of Chemistry,The Pennsylvania State University
• Associate Professor of Biochemistry and Molecular Biology,The Pennsylvania State University

EDUCATION:
• BA in Chemistry, Austin College (Sherman, TX), 1987
• PhD in Biochemistry, The Massachusetts Institute of Technology, 1994

HONORS & AWARDS:
• Presidential Early Career Award in Science and Engineering
• NSF Faculty Early Career Award
• NIH Postdoctoral Fellow
• NSF-NATO Postdoctoral Fellow

RESEARCH INTERESTS:
Enzymes carry out biochemical reactions with astronomical rate enhancements and amazing stereoselectivities, mediating the huge quantity and variety of cellular transformations that constitute what is vaguely termed 'life'. Our laboratory is endeavoring to understand at the detailed molecular level the reaction mechanisms employed by various enzymes, and then to exploit what we learn to impact favorably on human health and the human condition in general. A particular focus is to understand the manner in which enzymes bind and use cofactors — whether simple metal ions, complex metal clusters, or small molecules — to increase their catalytic capabilities beyond that which is supported by the functional groups of the twenty naturally occurring amino acids. To characterize enzymes and interrogate their modes of action, we use traditional biochemical and enzymological approaches in combination with structural methods such as X-ray crystallography and various forms of spectroscopy, as well as small-scale organic synthesis and fast-reaction kinetic methods. A growing interest in our lab has been to understand the mechanisms of enzymes that catalyze post-translational modification of proteins by catalysis that proceeds through organic radical intermediates. Particular focus is on enzymes that use iron-sulfur clusters and/or S-adenosylmethionine in catalysis.

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