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Incorporation of an Asymmetric Mo-Fe-S Cluster as an Artificial Cofactor into Nitrogenase. | LitMetric

Nitrogenase employs a sophisticated electron transfer system and a Mo-Fe-S-C cofactor, designated the M-cluster [(cit)MoFe S C]), to reduce atmospheric N to bioaccessible NH . Previously, we have shown that the cofactor-free form of nitrogenase can be repurposed as a protein scaffold for the incorporation of a synthetic Fe-S cluster [Fe S (SEt) ] . Here, we demonstrate the utility of an asymmetric Mo-Fe-S cluster [Cp*MoFe S (SH)] as an alternative artificial cofactor upon incorporation into the cofactor-free nitrogenase scaffold. The resultant semi-artificial enzyme catalytically reduces C H to C H , and CN into short-chain hydrocarbons, yet it is clearly distinct in activity from its [Fe S (SEt) ] -reconstituted counterpart, pointing to the possibility to employ molecular design and cluster synthesis strategies to further develop semi-artificial or artificial systems with desired catalytic activities.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9547968PMC
http://dx.doi.org/10.1002/cbic.202200384DOI Listing

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