Abstract
Nitrogenase is the only enzyme known to reduce nitrogen to ammonia. This intriguing enzyme is typically studied spectroscopically and due to the complexity of the nitrogenase system (including the dynamics of both a catalytic protein containing a FeMo-cofactor and an Fe protein), it is hard to directly study enzyme mechanism with standard spectroscopic techniques. This talk will discuss electroanalytical techniques for studying the enzyme mechanism of nitrogenase, including mediated bioelectrocatalysis and direct bioelectrocatalysis. The talk will discuss materials innovation for interfacing these complex proteins with electrode surfaces as well as the use of square wave voltammetry and amperometric titrations to evaluate mechanism, including inhibition studies, mutant enzyme studies, and kinetic isotope effect studies.
Published Version
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