Abstract

A suite of dynamic electrochemical techniques known as protein film electrochemistry (PFE) offers important insight into the roles of active sites in enzymes, including properties of electron-transfer centers (individually or collectively), rates and dependences of catalytic electron transport, and binding and dissociation of inhibitors. In this chapter, we explain how PFE is used to investigate the properties of FeS clusters-centers lacking distinctive or convenient spectroscopic signatures that are often very sensitive to O2. We see that PFE allows simultaneous detection and control of the reactions of individual FeS clusters, and measurement of their relaying efficiency in long-range electron transfer.

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