ABSTRACT
Electron transfer proteins serve key roles as electron carriers in a wide variety of processes in all organisms, including the major energy-transducing functions of photosynthesis and respiration, other metabolic functions such as nitrogen fixation, and biosynthesis [1]. One of the most intriguing questions about these proteins is that of how the protein itself influences the electron transfer properties of its redox site. In this chapter, computational methods used to understand the donor-acceptor energetic interactions of electron transfer proteins at a molecular level are described. The focus is on the electron transfer metalloproteins, which are the blue copper proteins, the iron-sulfur proteins, and the cytochromes. However, many of the issues discussed are important for redox-active proteins and/or metalloproteins in general.
