Diffusion of electrons over distances on the order of 100 μm has been observed in crystals of
a small tetraheme cytochrome (STC) from Shewanella oneidensis [J. Huang et al. J. Am …

Rapid and directed electron transfer (ET) is essential for biological processes. While the
rates of ET over 1–2 nm in proteins can largely be described by simplified nonadiabatic …

A series of calculations is reported of the superexchange electronic matrix element between
donor and acceptor states in photoinduced long-distance electron-transfer reactions in …

Proteins achieve efficient energy storage and conversion through electron transfer along a
series of redox cofactors. Multiheme cytochromes are notable examples. These proteins …

Multiheme cytochromes attract much attention for their electron transport properties. These
proteins conduct electrons across bacterial cell walls and along extracellular filaments and …

Electron transfer between two cytochromes is generally pos-tulated to take placeonly
through the exposed heme edge. 1 If this is the case, the protein serves as an insulator. The …

Cristallographic studies have shown that the heme group of cytochrome c lies in a crevice of
the protein with an edge of the porphyrin ring located at the molecule surface. The …

To probe the factors that control biological electron transfer, we analyzed the electron self-
exchange reactions of cytochromes c, C551, and b5. Numerical analysis of the crystal …

A microscopic treatment of the energetics of electron transfer reactions in proteins and
aqueous environments is presented. Using this treatment we correlate the observed X-ray …

When ferricytochrome c is reduced by H atoms (produced by pulse radiolysis) at neutral pH
where it is in a closed protein configuration, a considerable percentage of the reduction …