Journal Article
Proceedings of the National Academy of Sciences, vol. 111, iss. 2, pp. 611-616, 2014
Authors
Marian Breuer, Kevin M. Rosso, Jochen Blumberger
Abstract
Significance
Certain bacteria use complex assemblies of multiheme proteins to shuttle electrons from the inside of the cell over distances exceeding 100 Å to extracellular substrates. Recently, the first crystal structure of a representative deca-heme protein was solved, but the mechanism of electron conduction remains difficult to probe experimentally. Here we provide detailed molecular-level insight into the kinetics and thermodynamics of charge conduction in this biological wire using high-performance computational tools. Our study reveals an evolutionary design principle of significance to an entire class of heme proteins involved in mediating electron flow between bacterial cells and their environment, a phenomenon both bearing great geochemical importance and opening up a multitude of potential biotechnological applications.
