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. Author manuscript; available in PMC: 2017 Nov 22.
Published in final edited form as: Biochemistry. 2016 Nov 14;55(46):6363–6374. doi: 10.1021/acs.biochem.6b00635

Figure 4.

Figure 4

Schematic comparison of facial triad coordination for the classes of NHFe enzymes that have a second-sphere residue hydrogen bonding to the coordinated carboxylate (αKG dependent enzymes, shown at left, and the extradiol dioxygenases), leading to monodentate coordination, and those without a hydrogen bonding residue (pterin dependent enzymes, shown at right, and the Rieske dioxygenases), which leads to bidentate carboxylate coordination.