Selenocyanate Derived Se-incorporation into the Nitrogenase Fe Protein Cluster

Overview

Journal Elife

Specialty Biology

Date 2022 Jul 29

PMID 35904245

Authors

Trixia M Buscagan

Jens T Kaiser

Douglas C Rees

Affiliations

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Abstract

The nitrogenase Fe protein mediates ATP-dependent electron transfer to the nitrogenase MoFe protein during nitrogen fixation, in addition to catalyzing MoFe protein-independent substrate (CO) reduction and facilitating MoFe protein metallocluster biosynthesis. The precise role(s) of the Fe protein FeS cluster in some of these processes remains ill-defined. Herein, we report crystallographic data demonstrating ATP-dependent chalcogenide exchange at the FeS cluster of the nitrogenase Fe protein when potassium selenocyanate is used as the selenium source, an unexpected result as the Fe protein cluster is not traditionally perceived as a site of substrate binding within nitrogenase. The observed chalcogenide exchange illustrates that this FeS cluster is capable of core substitution reactions under certain conditions, adding to the Fe protein's repertoire of unique properties.

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