Redox processes power various biological and chemical phenomena ranging from photosynthesis and respiration to industrial catalysis and fuel cells. In nature, such processes are mediated by redox-active proteins such as azurin, a member of the cupredoxin family. Just as a variety of batteries are needed to power different electronic devices, proteins with varied redox potentials are needed to drive different biological processes. Scientists would like to modify such proteins in a controlled way to exploit them in redox processes. But engineering redox proteins hasn’t been easy because a detailed understanding of how specific amino acid changes affect redox potentials and other protein properties has been elusive. Redox potentials of copper complexes have previously been modified by changing solvents or pH.
by Stu Borman |
November 16, 2009