Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase
Name
elife-39451-v1.pdf
Description
Published version
Size
2.8 MB
Format
Adobe PDF
Checksum (MD5)
e73f8efc5f6278dc5426454476ee3c8d
Author(s)
Wittenborn, Elizabeth Charlot
Drennan, Catherine L
Date Issued
October 2018
Journal
eLife
Publisher
eLife Sciences Publications, Ltd
Citation
Wittenborn, Elizabeth C. et al. “Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase.” eLife, vol. 2018, 2018, e39451 © 2018 The Author(s)
Version
Final published version
Abstract
The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO 2 to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have observed unprecedented conformational dynamics in the C-cluster of the CODH from Desulfovibrio vulgaris, providing the first view of an oxidized state of the cluster. Combined with supporting spectroscopic data, our structures reveal that this novel, oxidized cluster arrangement plays a role in avoiding irreversible oxidative degradation at the C-cluster. Furthermore, mutagenesis of a conserved cysteine residue that binds the C-cluster in the oxidized state but not in the reduced state suggests that the oxidized conformation could be important for proper cluster assembly, in particular Ni incorporation. Together, these results lay a foundation for future investigations of C-cluster activation and assembly, and contribute to an emerging paradigm of metallocluster plasticity.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution 4.0 International license
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DOI of Published Version
https://doi.org/10.7554/ELIFE.39451
