About

Dmitry Matyushov is a professor of physics and chemistry at Arizona State University with research interests in theoretical and computational condensed matter physics, physical chemistry, and biophysics. His academic background includes an undergraduate degree from the Moscow Institute of Physics and Technology in 1986, a doctorate in theoretical physics from Kiev State University and the Ukrainian Academy of Sciences in 1989, and postdoctoral work in Vienna and at the University of Utah. His research encompasses spectroscopy, solvation, phase and glass transitions, complex fluids, electron transfer, dielectric spectroscopy, and bioenergetics, with current focus on protein dynamics, electrostatics of the protein-water interface, and problems related to ergodicity breaking and non-equilibrium ensembles in biology and enzyme catalysis.

Research topics

• Computer Science
• Physics
• Chemical physics
• Political Science
• Chemistry
• Condensed matter physics
• Physical chemistry
• Materials science
• Quantum mechanics
• Mechanics
• Geometry
• Inorganic chemistry
• Nanotechnology
• Optics
• Acoustics
• Photochemistry
• Optoelectronics
• Statistical physics

Selected publications

• Dynamics of low-temperature water are driven by electrostatics

  The Journal of Chemical Physics · 2026-04-08 · 1 citations

  articleSenior author

  Non-Gaussian dynamics in low-temperature liquids are assigned to spatial fluctuations of relaxation times and linear transport coefficients (dynamic heterogeneity). In contrast, molecular dynamics simulations of SPC/E water assign non-Gaussian dynamics to electrostatic intermolecular interactions growing in prominence with lowering temperature. Translational non-Gaussian parameters and rotational/translational relaxation times follow master curves produced by either changing temperature or the liquid's dipole moment. Static and dynamic compensation relations found for bulk water are assigned to the separation of time scales between density and electrostatic fluctuations.

  PublisherDOI

• Protein Electron Transfer in Solution, Protein Powders, and Electrode Confinement

  ACS Omega · 2026-02-12

  articleOpen accessSenior authorCorresponding

  Transport of electrons in biological electron transport chains involves interfaces and confinement, while measurements of rates of protein electron transfer and computer simulations are mostly conducted in solutions. Here, we employ molecular dynamics simulations of the azurin protein to compare activation parameters of electron transfer in solution with the corresponding parameters in confinement. We study the redox chemistry of azurin in protein powders and in confinement between two gold slabs, modeling conditions of an electrochemical experiment. The polarizability of the active site of the protein is included in the calculations and is found to be the main factor in lowering the reaction activation barrier. It couples to strong and inhomogeneous electric fields in confinement and protein powders, resulting in an observable reorganization energy of ∼0.1–0.2 eV, comparable to electrochemical measurements. Corresponding low activation barriers, ∼2kBT, yield a weak temperature effect on the reaction rate. No dynamical medium control of protein half-reactions is found in our calculations, producing rate constants exponentially decaying with the distance to the electrode.

  PublisherDOI

• Rotational memory function of SPC/E water

  The Journal of Chemical Physics · 2026-05-05

  articleSenior author

  Memory effects are essential for the dynamics of condensed materials and are responsible for non-exponential relaxation of correlation functions of dynamic variables through the memory function. Memory functions of dipole rotations for water have never been calculated directly from molecular dynamics simulations. We present here calculations of memory functions for single-dipole rotations and for the overall dipole moment of the sample for SPC/E water. The normalized memory functions for single-particle and collective dipole dynamics turn out to be nearly identical. This result validates theories of dielectric spectroscopy in terms of single-particle time correlation functions and the connection between the collective and single-particle relaxation times through the Kirkwood factor. The dielectric function in this formalism contains no new dynamic information that does not exist in the single-dipole correlation function. A short memory time, ≲1 fs, justifies the use of the mathematics of rotational diffusion to describe the dynamics of a single molecular dipole moment in bulk water. An analytical equation for the rotational memory time is derived.

  PublisherDOI

• BPS2026 – Photosynthetic reaction center: A nonergodic, dynamically anisotropic, and nonlinear charge-transport engine

  Biophysical Journal · 2026-02-01

  articleSenior author
  PublisherDOI

• Rotational Memory Function of SPC/E water

  ArXiv.org · 2026-01-15

  articleOpen accessSenior author

  Memory effects are essential for dynamics of condensed materials and are responsible for non-exponential relaxation of correlation functions of dynamic variables through the memory function. Memory functions of dipole rotations for polar liquids have never been calculated. We present here calculations of memory functions for single-dipole rotations and for the overall dipole moment of the sample for SPC/E water. The memory functions for single-particle and collective dipole dynamics turn out to be nearly identical. This result validates theories of dielectric spectroscopy in terms of single-particle time correlation functions and the connection between the collective and single-particle relaxation times through the Kirkwood factor. The dielectric function in this formalism contains no new dynamic information that does not exist in the single-dipole correlation function. A short memory time, $\lesssim 1$ fs, justifies the use of rotational diffusion model to describe dynamics of a single molecular dipole moment in bulk water.

  PublisherOA PDF

• Rotational Memory Function of SPC/E water

  arXiv (Cornell University) · 2026-01-15

  preprintOpen accessSenior author

  Memory effects are essential for dynamics of condensed materials and are responsible for non-exponential relaxation of correlation functions of dynamic variables through the memory function. Memory functions of dipole rotations for polar liquids have never been calculated. We present here calculations of memory functions for single-dipole rotations and for the overall dipole moment of the sample for SPC/E water. The memory functions for single-particle and collective dipole dynamics turn out to be nearly identical. This result validates theories of dielectric spectroscopy in terms of single-particle time correlation functions and the connection between the collective and single-particle relaxation times through the Kirkwood factor. The dielectric function in this formalism contains no new dynamic information that does not exist in the single-dipole correlation function. A short memory time, $\lesssim 1$ fs, justifies the use of rotational diffusion model to describe dynamics of a single molecular dipole moment in bulk water.

  PublisherDOI

• Photosynthetic Reaction Center: A Nonergodic, Dynamically Anisotropic, and Nonlinear Charge-Transport Engine

  The Journal of Physical Chemistry Letters · 2025-10-09

  articleSenior authorCorresponding

  We ask the question of what is special about photosynthetic reaction center proteins as media for transporting electrons across the lipid membrane. Ergodicity is broken down for the statistics of electrostatic fluctuations in the heliobacterial reaction center studied here by atomistic simulations. It is not restored on the simulation time scale of ∼1 μs, and it allows low activation barriers for electron hops. The medium dynamics are highly anisotropic (depending on the oxidation state) at cofactor sites, allowing a unidirectional flow of charge. This nonlinear protein response to altering the oxidation state combines with the coupling of cofactor polarizabilities to strong intraprotein electric fields to produce nonparabolic and nonergodic free-energy surfaces of electron transfer, allowing low-barrier charge conductivity in proteins.

  PublisherDOI

• Aqueous Ion Mobility over a Broad Concentration Range

  Physical Review Letters · 2025-06-11 · 2 citations

  articleSenior author

  For concentrations between dilute and the highly concentrated limit of almost 5 M, we compare our explicit-water molecular dynamics simulations of LiH_{2}PO_{4} (which dissociates into H_{2}PO_{4}^{-} anions relevant to biochemical processes and Li^{+} cations relevant to battery technology) to our pulsed-field gradient NMR measurements of ion diffusion, and find compensation between electrostatic and osmotic forces. The significance is that, noticing that the Kirkwood equation holds when using its exact solution but seemingly is violated when making the traditional approximation of using total force relaxation time in place of the memory relaxation time, we explain slower translational diffusion with increasing ion concentration as a dynamical effect arising from growing memory relaxation time. Physically, 2 orders of magnitude separate the timescales of electrostatic and osmotic forces from the total force such that dynamical correlations between force components lead to concentration-independent total force variance and force relaxation time.

  PublisherDOI

• Photosynthetic Reaction Center: A Nonergodic, Dynamically Anisotropic, and Nonlinear Charge-Transport Engine

  ChemRxiv · 2025-02-07

  preprintSenior author

  We ask the question of what is special about photosynthetic reaction-center proteins as media for transporting electrons across the lipid membrane. Ergodicity is broken for the statistics of electrostatic fluctuations in the heliobacterial reaction center studied here by atomistic simulations. It is not restored on the simulation time scale of ~ 1 us, and it allows low activation barriers for electron hops. The medium dynamics are highly anisotropic (depending on the oxidation state) at cofactors sites allowing unidirectional flow of charge. This nonlinear response of the protein to altering oxidation state combines with coupling of cofactor polarizabilities to strong intra-protein electric fields. Nonparabolic and nonergodic free energy surfaces of electron transfer allow low-barrier charge conductivity in proteins.

  PublisherDOI

• Memory function for protein diffusion

  The Journal of Chemical Physics · 2025-09-02

  articleSenior author

  Standard algorithms to calculate the diffusion constant from computer simulations are based on either the mean-squared displacement or the velocity autocorrelation function of the tagged particle. They register displacements/velocities caused by random forces, but do not address their physical nature. This deficiency is resolved in the force route to the diffusion constant leading to Kirkwood equation for massive diffusive particles (Brownian motion). Approximate Kirkwood equation becomes exact when the force relaxation time is replaced with the memory time. To formulate the force route to the diffusion constant, memory functions were calculated here from molecular dynamics simulations of six charge mutants of the green fluorescent protein and the plastocyanin protein in a wide range of temperatures. The memory time falls between the velocity and force relaxation times, with the Kirkwood equation overestimating diffusion constants of proteins by a factor of ∼4. Diffusion constants from the velocity/displacement route strongly increase with increasing system size. Standard protocols accounting for finite-size effects show serious flaws when applied to protein diffusion by producing system-size corrections far exceeding both the finite-size diffusion constants and their infinite-size extrapolations. Diffusion constants from the force route show much less system-size dependence, and corrected values are mostly independent of the system size.

  PublisherDOI

Recent grants

• Activated and nonlinear kinetics in biomolecules and interfaces

  NSF · $459k · 2018–2022

• Structure of water at interfaces with nanometer solutes and bioenergetics

  NSF · $281k · 2012–2015

• Electron transport in energy production complexes of biology

  NSF · $442k · 2015–2018

• Solvation and Electron Transfer in Anisotropic and Glassy Media

  NSF · $370k · 2006–2009

• Electrostatics at the nano-scale in application to protein solvation and function

  NSF · $405k · 2009–2013

Frequent coauthors

• Daniel R. Martin

  Arizona State University

  29 shared

• Marshall D. Newton

  Brookhaven National Laboratory

  24 shared

• Setare Mostajabi Sarhangi

  Arizona State University

  20 shared

• David N. LeBard

  18 shared

• Roland Schmid

  BMW (Germany)

  14 shared

• Mohammadhasan Dinpajooh

  Pacific Northwest National Laboratory

  14 shared

• Morteza M. Waskasi

  Roche (United States)

  13 shared

• Salman Seyedi

  12 shared

Education

• B.S., Chemical Physics

  Moscow Institute for Physics and Technology

  1985

• M.S., Chemical Physics

  National Ukrainian Academy of Sciences

  1986

• Ph.D., Theoretical Physics

  Kiev State University and National Ukrainian Academy of Sciences

  1989

Awards & honors

• Postdoctoral (Lise Meitner) fellowship from the Austrian Sci…