Abstract 1292 Using electrochemistry to control enzyme pathways

A significant fraction of enzymes are oxidoreductases that catalyze redox reactions. Although spectroscopy is the common method for evaluating enzyme kinetics, mechanism, and inhibition, spectroscopic techniques frequently require the use of "labels" or "chromophores" that may alter the kinetics and even the mechanisms of enzymes. This talk will discuss the use of electroanalytical techniques for studying enzymes. First, it will detail the use of mediated electron transfer mechanisms that similarly to spectroscopic assays require a secondary species that may interfere with kinetics and mechanism. Secondly, it will discuss electroanalytical techniques using direct electron transfer for more directly studying oxidoreductase enzymes. This paper will show the use of these strategies for enzymes ranging from laccase to nitrogenase in complexity and show that the kinetic rates and mechanism differ when "label-free"/direct systems are used for these enzymes. This work was funded by the National Science Foundation, the Department of Energy, and the Army Research Office MURI.