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• W2894881505 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 CO2 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." @default.
• W2894881505 created "2018-10-12" @default.
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• W2894881505 date "2018-10-02" @default.
• W2894881505 modified "2023-09-30" @default.
• W2894881505 title "Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase" @default.
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• W2894881505 doi "https://doi.org/10.7554/elife.39451" @default.
• W2894881505 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6168284" @default.
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