Multiheme cytochromes (MHCs) are bacterial electron-transfer proteins. We show from
optical spectra and calculations that some of these cytochromes probably contain occupied …

The naturally widespread process of electron transfer from metal reducing bacteria to
extracellular solid metal oxides entails unique biomolecular machinery optimized for long …

Multi-heme cytochromes (MHCs) are fascinating proteins used by bacterial organisms to
shuttle electrons within, between, and out of their cells. When placed in solid-state electronic …

Many species of bacteria can generate energy in the anoxic subsurface by directly coupling
intracellular oxidative reactions to the reduction of extracellular metal oxides. Coupling these …

The first three-dimensional structure of a dimeric, octa-heme cytochrome c 3 (M r 26000)
from Desulfovibrio desulfuricans Norway, established at 2.2 Å resolution, is briefly presented …

A method for calculating the electron-transfer matrix element V RP using density functional
theory Kohn− Sham orbitals is presented and applied to heme dimers of varying relative …

In this report, we analyze and interpret single-molecule current− voltage (I− V) tunneling
spectra collected for two decaheme c-type cytochromes using a scanning tunneling …

Multiheme cytochromes possess closely packed redox‐active hemes arranged as chains
spanning the tertiary structure. Here we describe five variants of a representative multiheme …

Bacteria of the genus Shewanella contain an abundant small tetraheme cytochrome in their
periplasm when growing anaerobically. Data collected for the protein isolated from S …

Distances between Fe ions in multiheme cytochromes are sufficiently short to make the
intramolecular dipole-dipole interaction between hemes probable. In the analysis of EPR …