Many biological functions are intrinsically light activated (e.g. photosynthesis or photoreceptors), and their study is a topic of intense ultrafast investigation. In contrast, most enzymes do not require light to function, even chromophore-containing enzymes like vitamins B6, B12, flavin or transition metal cluster enzymes. Nonetheless, ultrafast spectroscopies can be used to study these enzymes in several ways: e.g., a photon can surmount an activation barrier that is normally overcome thermally, vibrational modes can be directly accessed via infrared light ,or vibrational modes can be coherently activated and measured in the time-domain (e.g. quantum beats).
Currently, we are investigating:
- Light-Enhanced Catalysis by Pyridoxal Phosphate Dependent Aspartate Aminotransferase, Melissa P. Hill,Elizabeth C. Carroll, Mai C. Vang, Trevor A. Addington, Michael D. Toney and Delmar S. Larsen, J. AM. CHEM. SOC. 2010, 132 (47), 16953-16961 (2010) pdf
- Rapid Photodynamics of Vitamin B6 Coenzyme Pyridoxal 5'-Phosphate and its Schiff Bases in Solution, Melissa Hill, Elizabeth Carroll, Michael Toney, Delmar S. Larsen, Journal of Physical Chemistry B, 112 (18), 5867-5873 (2008). pdf
- A Single Source Femtosecond-Millisecond Broadband Spectrometer, Elizabeth Carroll, Melissa Hill, Dorte Madsen, Konstantin Malley, and Delmar S. Larsen Review of Scientific Instruments 80, 026102 (2009). pdf
- Multi-photon Manipulations of Enzymatic Photoactivity in Aspartate Aminotransferase, Melissa P. Hill, Lucy H. Freer, Mai C. Vang, Elizabeth C. Carroll, and Delmar S. Larsen, Journal of Physical Chemistry B, 115 (15), pp 4474–4483 (2011). pdf
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