Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
Name
nihms-1626948.pdf
Description
Accepted version
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2.22 MB
Format
Adobe PDF
Checksum (MD5)
57f9065beee006ea0931c42f0e1fbd9a
Author(s)
Cohen, Steven E
Brignole, Edward J
Wittenborn, Elizabeth C
Can, Mehmet
Thompson, Samuel
Ragsdale, Stephen W
Drennan, Catherine L
Date Issued
2021
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
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.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Massachusetts Institute of Technology. Department of Biology
Howard Hughes Medical Institute
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/J.STR.2020.08.011
