https://zenodo.org/record/1258475/files/article.pdf

Electron transfers in chemistry and biology

A major revival in the use of classical electrostatics as an approach to the study of charged and polar molecules in aqueous solution has been made possible through the development of fast numerical and computational methods to solve the Poisson-Boltzmann equation for solute molecules that have complex shapes and charge distributions. Graphical visualization of the calculated electrostatic potentials generated by proteins and nucleic acids has revealed insights into the role of electrostatic interactions in a wide range of biological phenomena. Classical electrostatics has also proved to be successful quantitative tool yielding accurate descriptions of electrical potentials, diffusion limited processes, pH-dependent properties of proteins, ionic strength-dependent phenomena, and the solvation free energies of organic molecules.

https://science.sciencemag.org/content/sci/268/5214/1144.full.pdf

Classical Electrostatics in Biology and Chemistry

Direct electrochemistry of redox proteins

In a redox enzyme the functional electron transfer center, normally surrounded by an insulating protein matrix, can be electrically connected to an external source of current through a path of fast electron-relaying redox couples. Such “wiring” is achieved through electrostatically or covalently binding to the enzyme-proteins high molecular weight redox polycations having segments anchored to electrodes. With the wired enzymes subsecond response time amperometric biosensors can be built.

Electrical Wiring of Redox Enzymes

The goal of this paper is to obtain a theoretical estimate of the dielectric constant of a folded protein. To this end, we develop a form of the Kirkwood–Frohlich dielectric theory that applies to polar solids and folded proteins. The resulting theory incorporates a factor expressing the degree to which dipolar groups are constrained within the material's structure, as well as a generalized form of Kirkwood's correlation factor. The theory is applied to a hypothetical isotropic protein composed of randomly oriented α-helices and having a number density of dipolar groups equal to that found in actual proteins. The factor of constraint and the generalized dipole correlation factor are calculated using normal mode analysis. Temperature factors are also computed by normal mode analysis and are in reasonable agreement with those found experimentally. The computed dielectric constant is low; the best estimate is that it falls between 2.5 and 4.

E Margoliash

Papers

The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications.