 | Acta Crystallographica Section B Acta Crystallographica Section B STRUCTURAL SCIENCE, CRYSTAL ENGINEERING AND MATERIALS |
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![[Figure 1]](gp5059fig1mag.jpg)
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Figure 1
Examples of native and substituted CoII sites showing the dominance of His (with a large preference for NE over ND binding), Asp and Glu in the coordination spheres. Notice also Scys in the CoII site of nitrile hydratase and in the CoII-substituted sites of type 1 copper proteins (exemplified here with pseudoazurin) and of zinc-dependent metallo-β-lactamases (exemplified with B. cereus BcII). S atoms also bind from methionine ligands in CoII-substituted type 1 copper sites and from post-translational derivatives of cysteine residues as observed in the native site of nitrile hydratase. Notice also the diversity in coordination numbers, the existence of mononuclear and binuclear sites, and in the latter case the possibility of single-atom (Owat) and three-atom (carboxylate-mediated) bridges. Arrow notations indicate which native ions are substituted in non-native CoII sites. Abbreviations: H-2,3-Dioxygenase = homoprotocatechuate 2,3-dioxygenase, ACMESD = α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase, MBL = metallo-β-lactamase. |
![[Figure 1]](gp5059fig1.jpg)
| STRUCTURAL SCIENCE CRYSTAL ENGINEERING MATERIALS |
ISSN: 2052-5206
