Sharon Hammes-Schiffer is the John Gamble Kirkwood Professor of Chemistry at Yale University. She is a theoretical chemist recognized for her work on chemical and biological reactions. She is known particularly for her theories of hydrogen tunneling and proton-coupled electron transfer and her studies of electrochemical, photochemical, and enzymatic processes. Hammes-Schiffer was born in Ithaca, New York in 1966. She graduated from Princeton University with a degree in chemistry in 1988 and received a doctorate from Stanford University in 1993. She pursued her postdoctoral studies at AT&T Bell Laboratories and was on the faculty of the University of Notre Dame, Pennsylvania State University, and University of Illinois Urbana-Champaign before joining Yale University in 2018. Hammes-Schiffer has been Chair of the Physical Division of the American Chemical Society, Deputy Editor of the Journal of Physical Chemistry B, Editor-in-Chief of Chemical Reviews, a member of the Basic Energy Sciences Advisory Committee for the Department of Energy, a member of the American Academy of Arts and Sciences, and a member of the International Academy of Quantum Molecular Science.

Research Interests

Hammes-Schiffer's research centers on the investigation of charge transfer reactions, dynamics, and quantum mechanical effects in chemical, biological, and interfacial processes. Her work encompasses the development of analytical theories and computational methods, as well as applications to a wide range of experimentally relevant systems. She has developed quantum mechanical and hybrid quantum-classical theories for proton-coupled electron transfer reactions, hydrogen tunneling in solution and enzymes, and fundamental electron-proton interactions and non-Born-Oppenheimer effects. Her calculations have assisted in the interpretation of experimental data and have provided predictions of rates and hydrogen/deuterium kinetic isotope effects. Her biological simulations have elucidated the roles of hydrogen tunneling, electrostatics, and protein motion in enzyme catalysis, as well as the impact of distal mutations. She and her collaborators proposed that equilibrium conformational changes and fluctuations throughout the protein facilitate enzyme catalysis. In conjunction with experimental collaborators, her calculations of proton-coupled electron transfer in molecular electrocatalysts are guiding the design of more effective catalysts for energy conversion processes relevant to solar energy devices.

Membership Type


Election Year


Primary Section

Section 14: Chemistry

Secondary Section

Section 29: Biophysics and Computational Biology