Akif Tezcan
Bioinorganic and biophysical chemistry; Metalloprotein structure, function and biosynthesis; Biomaterials
Bioinorganic and biophysical chemistry; Metalloprotein structure, function and biosynthesis; Biomaterials
Contact Information
Associate Professor of Chemistry and Biochemistry
Office: Urey Hall 6202
Phone: 858-534-4862
Email: tezcan@ucsd.edu
Web: tezcan.ucsd.edu
Group: View group members
Office: Urey Hall 6202
Phone: 858-534-4862
Email: tezcan@ucsd.edu
Web: tezcan.ucsd.edu
Group: View group members
Education
2001 Ph.D., , California Institute of Technology
1995 B.A., , Macalester College
2001 Ph.D., , California Institute of Technology
1995 B.A., , Macalester College
Awards and Academic Honors
2012
Frasch Foundation Award
2011
Saltman Lecture Award
2010
Sloan Research Fellowship
2008
Beckman Young Investigator Award
2007
NSF CAREER Award
2005
Chris and Warren Hellman Faculty Scholar
2001-2005
Burroughs-Wellcome and Helen Hay Whitney Postdoctoral Fellow, California Institute of Technology
2001
Herbert Newby McKoy Award for Graduate Research
Research Interests
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.
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.
Primary Research Area
Inorganic Chemistry
Inorganic Chemistry
Interdisciplinary interests
Biophysics
Macromolecular Structure
Materials
Macromolecular Structure
Materials
Image Gallery
Selected Publications
- "ATP-Uncoupled, Six-Electron Photoreduction of Hydrogen Cyanide to Methane by the Molybdenum-Iron Protein" with L. Roth, J. Am. Chem. Soc., 134, 8416-8419 (2012)
- "Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays" with J. Brodin, X. Ambroggio, C. Tang, K. Parent, T. Baker, Nat. Chem., 4, 375-382 (2012)
- "Expanding the Utility of Proteins as Platforms for Coordination Chemistry" with R.J. Radford, J.D. Brodin and E.N. Salgado, Coord. Chem. Rev., 255, 790-803 (2011)
- "Porous Protein Frameworks with Unsaturated Metal Centers in Sterically Encumbered Coordination Sites" with R.J. Radford. M. Lawrenz, P.C. Nguyen and J.A. McCammon, Chem. Comm., 47, 313-315 (2011)
- "ATP- and Iron Protein-Independent Activation of Nitrogenase Catalysis by Light" with L.E. Roth and J.C.Nguyen, J. Am. Chem. Soc.,132, 13672-13674 (2010)
- "Controlled Protein Dimerization through Hybrid Coordination Motifs" with R. Radford, P. Nguyen, T. Ditri and J. Figueroa, Inorg. Chem, 49, 4362-4369 (2010)
- "Evolution of Metal Selectivity in Templated Protein Interfaces" with J. Brodin, A. Medina-Morales, T. Ni, E. Salgado, X. Ambroggio, J. Am. Chem. Soc., 132, 8610-8617 (2010)
- "Metal Templated Engineering of Protein Interfaces" With E.Salgado, X.Ambroggio, J. Brodin, R. Lewis, B. Kuhlman. Proc. Natl. Acad.Sci. USA, 107, 1827-1832 (2010)
- "Metal-Directed Protein Self Assembly" With E.Salgado and R. Radford. Acc. Chem. Res., 43, 661-672 (2010).
- Structural Characterization of Microperoxidase inside a Metal-Directed Protein Cage, with T.Ni, Angew. Chem. Int. Ed., 49, 7014-7018 (2010)