The 2003 Benjamin Franklin medal in chemistry for pioneering the development of ultra-fast and multi-dimensional spectroscopies and their applications is presented to Robin M. Hochstrasser

• Published in: Journal of the Franklin Institute Vol. 341; no. 3; pp. 197 - 205
• Main Author: Grey, Roger A.
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.05.2004
• ISSN: 0016-0032; 1879-2693
• DOI: 10.1016/j.jfranklin.2003.12.015

Throughout his distinguished career of over 40 years, Robin Hochstrasser has made significant contributions to several areas of science in the fields of chemical and biochemical physics. He has been at the forefront and made fundamental contributions to the fields of photochemistry, solid-state chemistry, ultra-fast laser spectroscopies, and protein dynamics. He has been a prolific researcher, producing over 560 publications. His work has been characterized by experts in the fields as “a constant stream of experiments of lasting significance” (J. Phys. Chem. 100 (1996) 11791). Robin began his career in the 1960s using a variety of magnetic and electric field measurements to study crystals at low temperatures to understand spin quantization in solids and electron exchanged-mediated energy transfer. This work, described as a “classic contribution” (J. Phys. Chem. 100 (1996) 11791) was the basis for much of the subsequent experimental and theoretical work on the effect of magnetic fields on molecular spectra and on the measurements of dipole moments. In the late 1970s, Robin recognized the power of laser technology for the study of molecules and soon became a leader in the field investigating solid, gas phase, and condensed phase systems. He developed and applied various ultra-fast laser techniques to study the structure and dynamics of complex molecules in liquid phase, chemical, and biochemical reactions. He made seminal contributions to the development of two-dimensional infrared spectroscopy (2D IR) on a time scale of a picosecond or less. This 2D IR spectroscopy measures coupling between two functional groups in a large molecule and can thus be used to measure distances, as for example, two amide carbonyl groups in a peptide molecule. On the ultra-fast timescale, one application of 2D IR is to gain information on the rate of protein folding and unfolding in solution. Some of Robin's greatest contributions to understanding biomolecules are said to be in the experimental studies on the picosecond and femtosecond dynamics of heme proteins. Using techniques he developed he was able to observe the interactions of oxygen, carbon monoxide, and nitric oxide with hemoglobin inside the protein.