RESEARCH AREAS

Oleg Poluektov

Oleg Poluektov Chemical Sciences and Engineering Division Argonne National Laboratory P: 630-252-3546 E: oleg@anl.gov   M.S., Moscow Institute of Physics and Technology, 1980; Ph.D., Moscow Institute of Physics and Technology, 1983

Biographical Sketch

• 2000-present: Chemist, Chemistry Division, Argonne National Laboratory
• 1999: Visiting Scientist, Chemistry Division, Argonne National Laboratory
• 1997-1998: Visiting Scientist, Chemistry Division, Argonne National Laboratory
• 1991-1996: Visiting Scientist, Department of Physics, Leiden University, The Netherlands
• 1989-2000: Senior Scientist, Institute of Chemical Physics, Russian Academy of Sciences, Moscow
• 1983-1989: Scientist, Institute of Chemical Physics, Russian Academy of Sciences, Moscow

Research Statement

Natural photosynthetic conversion of solar energy to chemical energy is a unique phenomenon which sustains life on Earth.  The key step of photosynthetic energy conversion involves rapid, photoinduced sequential electron transfers resulting in efficient charge separation across a biological membrane. Fundamental to fully understanding these electron transfer events is discerning the involvement of heterogeneous polypeptide environments surrounding the redox cofactor sites.  High-resolution X-ray crystal structures of reaction center (RC) proteins reveal the structure of cofactors and surrounding protein environments, however, static crystallographic protein structures do not readily yield details of how native dynamic solution protein structures fine-tune electron transfer processes and coupled reactions, such as proton transfer.  Thus, novel approaches complementary to crystallography are required to experimentally correlate structural, electrostatic, and dynamic features of localized protein environments with inherent electron transfer reactions.

In our research we utilize a suite of advanced, multi-frequency, time-resolved EPR resonance techniques in combination with specialized samples. The center piece of these advanced techniques is high-frequency, pulsed, 130 GHz EPR spectroscopy which demonstrates a unique high absolute sensitivity and high spectral resolution compared to conventional 9 GHz EPR spectroscopy.

The ultimate goal of our photosynthetic research is to obtain fundamental knowledge of how photochemical processes at the molecular level are linked to the chemistry of macroscopic energy conversion. Specifically our research related to the protein’s role in controlling and defining optimal pathways for ET reactions; the response of the protein to rapid charge transfer and separation; and local metal and cofactor site structure related to conformationally gated ET.  This knowledge is crucial for the future design and optimization of novel biomimetic and model artificial solar energy conversion systems.