Iron-sulfur clusters are one of the most ancient, versatile and multi-functional prosthetic groups found in biology. They are commonly involved in essential biological processes in living cells, such as electron transfer, catalysis, regulatory sensing, and many more. Here, we present our recent Mössbauer and EPR studies of novel [4Fe-4S] clusters resided in NifB enzyme, an S-adenosylmethionine dependent enzyme that is a key biosynthetic hub for the unique iron-molybdenum cofactor of nitrogenase. Spectroscopic analyses on samples obtained from different genetic background revealed the spectroscopic features of different [4Fe-4S] clusters present in the protein scaffold and their different ligation environment. Spectroscopic analyses also revealed evidence for the existense of an iron-sulfur cluster exhibiting an S &gt; 5/2 spin ground state in the wild-type NifB protein.These results will be used to discuss potential functions of these iron-sulfur clusters in NifB.

Mössbauer and EPR studies of novel iron-sulfur clusters

ACS Spring 2022

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