4:30pm - 5:30pm
Room 209 Havemeyer Hall
New York, NY 10027
Hosted by the Chemistry Graduate Students
In photosynthetic light harvesting, absorbed energy migrates through a protein network to reach a dedicated location for conversion to chemical energy. This energy flow is efficient, directional, and, in oxygenic photosynthesis, regulated. The regulatory response, known as non-photochemical quenching (NPQ), safely dissipates excess energy to protect the system against deleterious photoproducts. In recent research, a protein within this network, light- harvesting complex stress related (LHCSR), has been implicated in dissipation in green algae and moss, yet the mechanisms of photoprotection remain poorly understood. We explore these mechanisms with single-molecule spectroscopy of LHCSR. By characterizing the conformational dynamics, we identify the extent of energy dissipation in single LHCSR proteins and how this changes under conditions that mimic high and low light. While this approach reveals the conformational dynamics of solubilized photosynthetic proteins, we also present experiments measuring ultrafast energy transfer dynamics for proteins held within a near-native membrane environment. Together, these experiments explore how the protein network produces an efficient and adaptable energy flow.
Wednesday, October 26, 2016 at 4:30pm
Room 209 Havemeyer
***PLEASE NOTE SPECIAL DAY!***
Tea and cookies will be served prior to the lecture at 4:00pm in the Miller Room 328 Havemeyer.
Department of Chemistry, Columbia University, Havemeyer Hall, 3000 Broadway, New York, NY 10027, USA | 212-854-2202 | http://chem.columbia.edu/