Catechol deoxy state

In 1998, Krebs and co-authors reported the crystal structures of the catechol oxidase isolated from sweet potatoes (Ipomoea batatas) in three catalytic states the native met (CunCun) state (Figure 5.2a), the reduced deoxy (Cu Cu1) form, and the complex with the inhibitor phenylthiourea (Figure 5.2b) [19]. Typically for the type 3 active site, each copper ion is coordinated by three histidine residues from the protein backbone. In the native met state, the two copper ions are 2.9 A apart and, in addition to six histidine residues, a bridging solvent molecule, most likely a hydroxide anion, has been refined in close proximity to the two metal centers... 

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