DMITRY MATYUSHOV

Professor
Ph.D., Kiev's State University (Ukraine), 1989

  Office: PSF-359B  
  Phone: (480)965-0057  
  Fax: (480) 965-2747
  Email: dmitrym@asu.edu

 Dr. DMITRY MATYUSHOV's Lab or Group Website

Research and Teaching Interests

Bacterial reaction center in a micellar detergent and water generated by computer simulation [J. Phys. Chem. 112 (2008) pp. 10322–10342].

We are interested in understanding of how the energy is transferred in biology and molecular assemblies. Energy chains in biology rely on transmembrane transfer of redox energy from electron donating molecules to catalitic sites where the energy is stored in chemical bonds. A similar mechanism is realized in natural and artificial photosynthesis. The photon energy is first stored in a photoabsorbing molecule and is then transferred away from the point of primary photon absorption to an active site where some catalitic chemical process occurs. In all these mechanisms electron moves between centers of localization on organic cofactors or active sites of enzymes. We are working on understanding the kinetics and energetics of these elementary electron transport events with the goal of formulating the general principles of energetic efficiency of molecular charge-transfer chains. Our research strategy combines the use of computer simulations of realistic systems with the development of theoretical models which can be directly applied to interpreting the experimental data. Two areas of current research include electron transport in bacterial and artificial photosynthesis and the modeling of the electrostatics and dynamics of the protein-water interface.

Hydration shells around proteins are significantly polarized producing non-Gaussain enectrostatic fluctuations [J. Phys. Chem. 113 (2009) pp. 12424­-12437].

It has long been appreciated that the ability of proteins to participate effectively in the energetic chains of biology is linked to the electrostatics of proteins themselves and the hydration shells of water. The standard textbook description of the local protein polarity ascribes it a low dielectric constant comparable to that of chloroform. Large-scale computer simulations show that this is only partially true. Proteins have a broad distribution of relaxation times and, depending on the process of interest, can be either non-polar or very polar. This feature of polarity switch directly applies to the energetics of bacterial photosynthesis where charge separation reactions occur on short, picosecond times revealing non-polar protein environment while recombination reactions occur on the longer, nanosecond times switching to a strongly polar response of the protein. This latter polar response is characterized by a significantly non-Gaussian statistics of the electrostatic fluctuations. This property, directly observed in MD simulations, can potentially explain how nature performs multiple hops of electrons in its energy chains without loosing all the input energy initiated by either the incoming photon or a redox reaction.

Publications

"Solvated dissipative electro-elastic network model of hydrated proteins," Daniel R. Martin and Dmitry V. Matyushov, J. Chem. Phys. 137 165101 (2012)

"Protein-water electrostatics and principles of bioenergetics," David N. LeBard and Dmitry V. Matyushov, Phys. Chem. Chem. Phys. 12 15335-15348 (2010)

"Energetics of Electron Transfer Reactions in Soft Condensed Media ," D. V. Matyushov, Acc. Chem. Res. 40 294 (2007)

"Understanding the Optical Spectroscopy: Coumarin-153 Steady-State Spectroscopy," D.V. Matyushov and M.D. Newton, J. Phys. Chem. A 105 8516-8532 (2001)