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Scott Group Alumni Dr. Brian JustusDr. Kim Tran Dr. Mark Iannone Dr. Alan Huston Dr. Donald O'Connor Dr. Larry Talley Dr. Dariush Vosooghi Dr. David Boldridge |
Rooms 1444 and 1428 Pierce Hall
  Dr. Scott and his research group are studying photophysical and photochemical events in a variety of molecular systems and materials. They use both laser and conventional spectroscopic techniques to elucidate excited electronic state energetics and kinetics, charge and energy migration, nonlinear optical properties, and photochemistry in condensed media. Some of the techniques they employ include photochemical hole burning spectroscopy; time-resolved absorption and emission spectroscopy; femtosecond degenerate four-wave mixing spectroscopy; and fluorescence, fluorescence anisotropy and UV-vis absoption spectroscopy; and Raman, NMR, and FTIR spectroscopy. Temperature-dependent studies down to 1.5K are used. Current projects include: 1)Spectroscopic and Photochemical Studies of Aromatic Photodimers, 2) Linear and Nonlinear Spectroscopy of Excited Charge Transfer States, and 3) Self-regulation Effects in Biological Charge Transfer Systems. Currently, one postdoc, two graduate students, and one undergraduate student work in the lab. The lab is in the North wing of the Pierce Hall Chemistry Building, and close to the small parking lot for service vehicles.
People who work in the lab: Dr. Alexander "Sasha" Gouscha Sasha came to Riverside from Kyiv (Ukraine) where he worked in the Institute for Physics. Sasha worked also for three years in the Max-Planck Institute for Strahlenchemie, Muelheim an der Ruhr (Germany). His previous interdisciplinary scientific experience led him to Riverside, where the excellent research facilities and morvelous climate created favorable conditions to continue his research work. Sasha, his wife and two sons like Southern California with its strong academic environment, wonderful hiking surroundings and sailing opportunities. Sasha's main scientific interests cover non-equilibrium structural transition in proteins and their role in function of biomolecules. Among the currently studied systems are the photosynthetic reaction centers, photosynthetic oxygen evolving systems, cytochrome oxidases, and bacteriorhodopsins. These macromolecules, although different structurally and functionally, seem to obey the same physical principles in their function. In particular, our recent studies indicated the prime importance of non-equilibrium dynamic effects and non-equilibrium phase transitions in function of these biomolecules. Email address : goushcha@citrus.ucr.edu Darcy Tarrant My proposed research includes the photochemical investigation of the decomposition of polyacene dimers in perdeuterated dimer hosts. Laser induced fluorescence, one-and two-photon fluorescence excitation spectroscopy, fluorescence anisotropy measurements, as well as two color photochemical hole burning will be employed to study these systems. The information obtained in the interchromophoric coupling will be used to determine the type of interaction existing between chromophores and will aid in the development of a theoretical model to explain these interactions. The experimental and theoretical information will be used to assign the excited state energy levels in the molecules. These studies will lead to a more thorough understanding of the excited state interactions of aromatic dimers. Anthony Manzo Currently I'm working on experiments to measure photoexcitation and charge recombination kinetics in photosynthetic reaction centers with the intent to better understand the coupling of these events to the protein dynamics in these biomolecules. Such proteins are macromolecular complexes and can reveal physical principles behind the behavior of similar complex systems in general. Such studies may also lead to important technological uses of proteins as complex adaptive materials. Email: manzoa01@student.ucr.edu Sherlyn Ann Benois-Green Sherlyn is currently an undergraduate here. She is studying charge transfer and charge recombination in the protein cytochrome oxidase within sol-gel glasses. With this method charge recombination in an intramolecular system can be studied through immobilized proteins opposed to an intermolecular system where proteins are allowed to interact with one another in aqueous solution. Proteins that are encapsulated within the caverns of the sol-gel matrix will not be able to come in contact with other macromolecules in that environment, so viewing how this particular protein will adapt to those conditions will be viewed as well. Email: benois01@student.ucr.edu
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|   | This page was prepared by Professor Scott's group. In the background is the dipentacene molecule. Last updated on 6/19/00. |