Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase
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 i...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications, Ltd
2020
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| Online Access: | https://hdl.handle.net/1721.1/126196 |
| _version_ | 1826209468599238656 |
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| author | Wittenborn, Elizabeth Charlot Drennan, Catherine L |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Wittenborn, Elizabeth Charlot Drennan, Catherine L |
| author_sort | Wittenborn, Elizabeth Charlot |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T14:22:59Z |
| format | Article |
| id | mit-1721.1/126196 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T14:22:59Z |
| publishDate | 2020 |
| publisher | eLife Sciences Publications, Ltd |
| record_format | dspace |
| spelling | mit-1721.1/1261962022-09-29T09:07:16Z Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase Wittenborn, Elizabeth Charlot Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry 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. National Institutes of Health (U.S.) (Grant R01 GM069857) National Institutes of Health (U.S.) (Grant T32 GM008334) National Institutes of Health (U.S.) (Grant R35 GM126982) 2020-07-15T13:57:10Z 2020-07-15T13:57:10Z 2018-10 2018-06 2019-12-03T18:54:00Z Article http://purl.org/eprint/type/JournalArticle 1534-4983 https://hdl.handle.net/1721.1/126196 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) en 10.7554/ELIFE.39451 eLife Creative Commons Attribution 4.0 International license https://creativecommons.org/licenses/by/4.0/ application/pdf eLife Sciences Publications, Ltd eLife |
| spellingShingle | Wittenborn, Elizabeth Charlot Drennan, Catherine L Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase |
| title | Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase |
| title_full | Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase |
| title_fullStr | Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase |
| title_full_unstemmed | Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase |
| title_short | Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase |
| title_sort | redox dependent rearrangements of the nifes cluster of carbon monoxide dehydrogenase |
| url | https://hdl.handle.net/1721.1/126196 |
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