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EC Number
Metals/Ions
Commentary
Reference
Cu2+
the active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
Cu2+
the calculated dissociation energies suggest that the reactive intermediate is either a Cu(II)-oxyl, a Cu(III)-oxyl, or a Cu(III)-hydroxide, indicating that O-O bond breaking occurs before the C-H activation step
Cu2+
The copper ion lies in the center of a flat surface that interacts with the substrate. The equatorial plane includes the protein's N-terminal Ndelta of His-1 and the Nepsilon of His-83
Cu2+
the copper site is highly similar to that of the C1/C4 cellulose-oxidizing LPMO9A from Thermoascus aurantiacus and exhibits an octahedral coordination geometry with Jahn-Teller distortion. Dissociation constant is 12 nM; the copper site of CelS2 is similar to that of chitin-active LPMO10s. Dissociation constant is 31 nM
Cu2+
the oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand
Cu2+
the reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose
Cu2+
type II copper center, which exhibits a hexacoordination
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