Upcoming Seminars & Events

Professor Akif Tezcan

Professor Akif Tezcan
Department of Chemistry & Biochemistry
University of California San Diego

Structural Insights into Biological Nitrogen Fixation

Reduced forms of nitrogen are essential for the biosynthesis of amino and nucleic acids as well as the production of fertilizers and many commodity chemicals. Nitrogenase is the only enzyme capable of reducing atmospheric nitrogen to ammonia and responsible for the sustenance of ~50% of the human population. This challenging reaction requires the coordinated transfer of multiple electrons from the reductase component, the Fe-protein, to the catalytic component, MoFe-protein, in an ATP-dependent fashion. Despite extensive research in the last five decades, however, the mechanistic details of ATP- dependent energy transduction and nitrogen reduction by nitrogenase are not well understood. Another outstanding question is how the highly sensitive metal clusters of nitrogenase are protected from oxygen in aerobic nitrogen-fixing organisms. In this presentation, I will discuss our group’s efforts toward addressing these mechanistic questions through a combination of photochemical, spectroscopic, and structural biology tools.

Akif Tezcan

Akif Tezcan is a Professor in the Department of Chemistry and the Materials Science and Engineering (MSE) Program at UCSD. He was educated at the German High School in Istanbul, Macalester College in St. Paul, MN (BA in Chemistry and Biology) and Caltech in Pasadena, CA, USA (PhD in Bioinorganic Chemistry with Harry Gray), followed by postdoctoral research at Caltech as a Helen Hay Whitney fellow (with Doug Rees). His research program at UCSD, started in 2005, focuses on developing new chemical tools and strategies to study biological nitrogen fixation, to design functional proteins and enzymes, and to create new protein-based materials. Akif’s research program at UCSD has been recognized with an NSF CAREER Award, Sloan Fellowship, Beckman Young Investigator Award, Frasch Foundation Award, Moore Distinguished Scholarship, the Early Career Award from the Society of Biological Inorganic Chemistry, Guggenheim Fellowship, and the ACS Alfred Bader Award in Bioinorganic Chemistry.

Professor Akif Tezcan

Professor Akif Tezcan
Department of Chemistry & Biochemistry
University of California San Diego

Chemical and Computational Design of Metalloenzymes

Motivated by a desire to build new bioinorganic functions beyond what nature has invented, we have developed chemical design approaches in which folded proteins are used as synthons for building supramolecular complexes through metal-mediated self-assembly. The interfaces in the resulting protein superstructures are subsequently tailored with covalent, non-covalent or additional metal-coordination interactions for stabilization and incorporation of new functionalities. This strategy has not only enabled the construction of functional metalloproteins and protein-based materials with unusual properties but also led to the discovery of fundamental design principles that govern the metal-protein interplay. In parallel, we have leveraged advances in AI/ML-based computational methods to design de novo metalloproteins with new-to-nature structures and metal centers with atomic accuracy, which have allowed access to diverse catalytic functions. This presentation will focus on selected examples of such designed metalloproteins from our laboratory.

Akif Tezcan

Professor Akif Tezcan

Professor Akif Tezcan
Department of Chemistry & Biochemistry
University of California San Diego

Chemical Strategies for Assembling Functional Protein-Based Materials

Proteins represent the most versatile building blocks available to living organisms or the laboratory scientist for constructing functional materials and molecular devices. Underlying this versatility is an immense structural and chemical heterogeneity that renders the programmable self-assembly of proteins an extremely challenging design task. To circumvent the challenge of designing extensive non-covalent interfaces for controlling protein self-assembly, our group has endeavored to use chemical bonding strategies based on fundamental principles of inorganic chemistry and molecular symmetry. These strategies (combined with some supramolecular and polymer chemistry) have resulted in discrete or infinite, 0-, 1-, 2- and 3D protein architectures that display high structural order over large length scales, yet are dynamic, adaptive and possess new emergent chemical/physical properties. This presentation will highlight some of these functional protein-based materials constructed in our laboratory.