Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Author(s)
Cohen, Steven E; Brignole, Edward J; Wittenborn, Elizabeth C; Can, Mehmet; Thompson, Samuel; ... Show more
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Abstract
© 2020 Elsevier Ltd Cohen et al. demonstrate that carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) undergoes wider conformational changes than previously reported. Furthermore, these new conformations explain how the ACS subunit can interact with corrinoid Fe-S protein (CFeSP) in order to mediate a methyl transfer reaction instrumental for anaerobic carbon fixation.
Date issued
2021
URI
https://hdl.handle.net/1721.1/139663
Department
Massachusetts Institute of Technology. Department of Chemistry; Massachusetts Institute of Technology. Department of Biology; Howard Hughes Medical Institute
Journal
Structure
Publisher
Elsevier BV
Citation
Cohen, Steven E, Brignole, Edward J, Wittenborn, Elizabeth C, Can, Mehmet, Thompson, Samuel et al. 2021. "Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase." Structure, 29 (1).
Version: Author's final manuscript
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