Selenocyanate derived Se-incorporation into the Nitrogenase Fe protein cluster
- Howard Hughes Medical Institute, California Institute of Technology, United States
- California Institute of Technology, United States
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 (CO2) reduction and facilitating MoFe protein metallocluster biosynthesis. The precise role(s) of the Fe protein Fe4S4 cluster in some of these processes remains ill-defined. Herein, we report crystallographic data demonstrating ATP-dependent chalcogenide exchange at the Fe4S4 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 Fe4S4 cluster is capable of core substitution reactions under certain conditions, adding to the Fe protein's repertoire of unique properties.
Data availability
Diffraction data have been deposited in the RCSB PDB under the accession codes 7TPW, 7TPX, 7TPY, 7TPZ, 7T4H, 7TQ0, 7TQ9, 7TQC, 7TNE, 7TQE, 7TQF, 7TPN, 7TQH, 7TQI, 7TPO, 7TQJ, 7TQK, and 7TPV.
Article and author information
Author details
Funding
Howard Hughes Medical Institute
- Douglas C Rees
National Institutes of Health (GM45162)
- Douglas C Rees
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2022, Buscagan et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Selenocyanate derived Se-incorporation into the Nitrogenase Fe protein cluster
eLife 11:e79311.
https://doi.org/10.7554/eLife.79311
Further reading
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