个人简介

2014 SBIC Early Career Award 2014 Moore Distinguished Scholar, Caltech 2012 Frasch Foundation Award 2011 Saltman Lecture Award 2010 Sloan Research Fellowship 2008 Beckman Young Investigator Award 2007 NSF CAREER Award

研究领域

Inorganic Chemistry

The projects in the Tezcan group focus on the elucidation of metal-catalyzed biological redox reactions, and the control of biological self-assembly through coordination chemistry. Metal-Directed Protein-Protein Interactions and Protein Self-Assembly: Protein-protein interactions (PPIs), whether formed transiently during signal transduction or permanently in macromolecular assemblies, are central to all cellular processes. The overarching goal of this multifaceted project is to develop tools based on inorganic coordination chemistry to guide protein-protein docking interactions, and apply them towards 1) the rational assembly of protein supramolecular structures and frameworks, 2) the evolution of functional metal centers in protein interfaces and 3) the control and interrogation of biological signaling pathways. Understanding Biological Nitrogen Fixation: The conversion of molecular nitrogen into bioavailable forms such as ammonia is essential for the biosynthesis of amino and nucleic acids, as well as the production of fertilizers and countless industrial chemicals. The extreme conditions required by the industrial nitrogen fixation processes, however, translate into an immense dependence on fossil fuels and account for 1-2% of all human energy consumption. Our goal in this project is to elucidate the molecular mechanism of nitrogenase, a redox-metalloenzyme that catalyzes nitrogen fixation at ambient conditions. In particular, we aim 1) to understand why and how ATP-hydrolysis is involved in nitrogen fixation, and 2) to drive the nitrogenase reaction by using light or electrochemical energy instead of ATP hydrolysis in order to achieve a better control and understanding of nitrogen-activation. All projects in the Tezcan Group are inspired by a deep appreciation of nature's ability to control and exploit the chemistry of metal ions. They utilize a diverse array of tools ranging from molecular biology, chemical synthesis and computational protein design to spectroscopy, X-ray crystallography and electron microscopy.

近期论文

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F. A. Tezcan, J. Kaiser, J. Howard, D. Rees "Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase", J. Am. Chem. Soc., 2015, Vol. 137, 146 C. Machan, S. Chabolla, J. Yin, M. Gilson, F. A. Tezcan, C. Kubiak "Supramolecular Assembly Promotes the Electrocatalytic Reduction of Carbon Dioxide by Re (I) Bipyridine Catalysts at a Lower Overpotential", J. Am. Chem. Soc, 2014, Vol. 136, 14598 J. Brodin, J. Carr, P. Sontz, F. A. Tezcan "Exceptionally stable, redox-active supramolecular protein assemblies with emergent properties", Proc. Natl. Acad. Sci., 2014, Vol. 111, 2897 P. Sontz, W. Song, F. A. Tezcan "Interfacial metal coordination in engineered protein and peptide assemblies", Curr. Opin. Chem. Biol., 2014, Vol. 19, 42 W. Song, F. A. Tezcan "A designed supramolecular protein assembly with in vivo enzymatic activity", Science, 2014, Vol. 346, 1525 W. Song, P. Sontz, F. A. Tezcan "Metals in protein-protein interfaces", Ann. Rev. Biophys., 2014, Vol. 43, 409 A. Medina Morales, A. Perez, J. Brodin, F. A. Tezcan "In vitro and cellular self-assembly of a Zn-binding protein cryptand via templated disulfide bonds", J. Am. Chem. Soc., 2013, Vol. 135, 12013 D. Huard, K. Kane, F. A. Tezcan "Re-engineering protein interfaces yields copper-inducible ferritin cage assembly", Nat. Chem. Biol., 2013, Vol. 9, 169-176 S. Smith, K. Du, R. Radford, F. A. Tezcan "Functional, metal-based crosslinkers for α-helix induction in short peptides", Chem. Sci., 2013, Vol. 4, 3740 J. Brodin, X. Ambroggio, C. Tang, K. Parent, T. Baker, F. A. Tezcan "Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays", Nat. Chem., 2012, Vol. 4, 375 L. Roth, F. A. Tezcan "ATP-Uncoupled, Six-Electron Photoreduction of Hydrogen Cyanide to Methane by the Molybdenum-Iron Protein", J. Am. Chem. Soc, 2012, Vol. 134, 8416