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
Accepting Rotation Students: Yes

2021

Guggenheim Fellow

2016

Ernest Swift Lectureship

2015

Kavli Frontiers Fellow

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

The overarching goal of the Tezcan Lab is to create and understand biological complexity through chemical and protein design approaches. Our research is motivated by the fact that proteins are the most versatile building blocks for the construction of biological machines (e.g., photosystem II, nitrogenase and cytochrome c oxidase) and advanced scaffolding materials (e.g., collagen superstructures, microtubules, viruses) that provide the necessary molecular components to sustain the complexity of living systems. However, the ability of laboratory scientists to control the self-assembly of proteins or to use them as synthetic building blocks has been limited owing to the chemical and structural complexity/heterogeneity of protein molecules. Inspired by fundamental principles of inorganic coordination chemistry and supramolecular chemistry, our group develops new chemical strategies for the construction of complex protein assemblies with sophisticated structures and physicochemical properties, and integrate such systems into living systems.

In parallel, we are interested in understanding the molecular details of 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 to understand why and how ATP-hydrolysis is involved in nitrogen fixation, and use this knowledge to drive the nitrogenase reaction by using light or electrochemical energy instead of ATP hydrolysis.

Work by the Tezcan Group spans all areas of chemistry and utilizes a diverse array of tools ranging from molecular biology, chemical synthesis, polymer science, and computational chemistry to X-ray crystallography, electron microscopy, spectroscopy and advanced materials characterization techniques.

Biophysics
Macromolecular Structure
Materials