Mechanism for electron transfer within and between proteins

Abstract

Examination of a growing range of electron transfer proteins is clarifying what design elements are and are not naturally selected. Intraprotein electron transfer between natural redox centers is generally engineered to be robust and resistant to mutational changes and thermal fluctuations, by using chains of redox centers connected by electron tunneling distances of 14 A or less. This assures that tunneling rates are faster than the typical millisecond bond-breaking at catalytic sites. Interprotein electron transfer addresses the potential problem of slow diffusion by designing attractive docking sites that permit a conformational search for short tunneling distances.