Faster Interprotein Electron Transfer in a [Myoglobin, b 5 ] Complex with a Redesigned Interface

Abstract

Speeding Electron Transfer Between Proteins Compared to those observed in photosynthetic proteins, electron transfer rates between other large biomolecules, such as myoglobin and cytochrome b 5 , are very slow. Xiong et al. (p. 1075 ) show that modifying the acidic amino acid residues in the binding surface of myoglobin to lysine changes the distribution of structures to ones that favor faster electron transfer from the zinc porphyrin in myoglobin to the heme iron of cytochrome b 5 . The rates observed are within an order of magnitude of those observed for the initial step of charge separation in photosynthesis and provide valuable data for scientists interested in designing reactive proteins.