Many enzymes utilize metallocofactors to catalyze chemical transformations that are important in creating a sustainable world.  The H-cluster of [FeFe]-Hydrogenase catalyzes the reversible production of molecular hydrogen and the M-cluster of Nitrogenase the reduction of dinitrogen to ammonia.  Insight into how these metallocofactors can catalyze such useful transformations has come through studying their biological assembly by radical S-adenosylmethionine (SAM) enzymes.  The radical SAM enzymes HydG and NifB play critical roles in transforming simple precursors into the complex metallocofactors found in [FeFe]-Hydrogenase and Nitrogenase respectively.  By using total and selective labeling of HydG and NifB with <sup>57</sup>Fe, important intermediates and products have been characterized by EPR and Mössbauer spectroscopies.  Results give a better understanding of how the electronic structure changes as these enzymes piece together these complex metallocofactors.

Characterization of the radical S-Adenosylmethionine (SAM) enzymes HydG and NifB by EPR and Mössbauer spectroscopies

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ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.