Electron-transporting multi-heme cytochromes are essential to the metabolism of microbes that inhabit soils and carry out important biogeochemical processes. Recently the first crystal structure of a prototype bacterial deca-heme cytochrome (MtrF) has been resolved and its electrochemistry characterized. However, the molecular details of electron transport along heme chains in the cytochrome are difficult to access via experiment due to the nearly identical chemical nature of the heme cofactors. Here we employ large-scale molecular dynamics simulations to compute the redox potentials of the 10 hemes of MtrF in aqueous solution. We find that as a whole they fall within a range of ~0.3 V, in agreement with experiment. Individual redox potentials give rise to a free energy profile for electron transport that is approximately symmetric with respect to the center of the protein. Our calculations indicate that there is no significant potential bias along the orthogonal octa- and tetra-heme chains, suggesting that under aqueous conditions MtrF is a nearly reversible two-dimensional conductor.