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. Author manuscript; available in PMC: 2017 Dec 1.
Published in final edited form as: Biochemistry. 2017 Feb 23;56(9):1248–1260. doi: 10.1021/acs.biochem.6b00983

Figure 1.

Figure 1

ACS active site determined by crystallography (PDB entry 1OAO, Moorella thermoacetica). “Closed” conformation (the access path from the CODH Ni–Fe center to the ACS active site is closed) showing Zn occupancy at the tetrahedral Nip site (left). “Open” conformation with Ni at the square-planar Nip site (right). The S–S–S–Ni dihedral angle demonstrates the change in geometry between the sites. A large difference in the Ni–metal distances is observed.