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

Authors :: Massachusetts Institute of Technology. Department of Chemistry
Massachusetts Institute of Technology. Department of Biology
Howard Hughes Medical Institute
Cohen, Steven E
Brignole, Edward J
Wittenborn, Elizabeth C
Can, Mehmet
Thompson, Samuel
Ragsdale, Stephen W
Drennan, Catherine L
Massachusetts Institute of Technology. Department of Chemistry
Massachusetts Institute of Technology. Department of Biology
Howard Hughes Medical Institute
Cohen, Steven E
Brignole, Edward J
Wittenborn, Elizabeth C
Can, Mehmet
Thompson, Samuel
Ragsdale, Stephen W
Drennan, Catherine L
Source :: PMC
Publication Year :: 2022
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.

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