1.14.99.56	Cu2+	-	
1.14.99.56	Cu2+	residue Tyr203 is placed approximately 15 A away from the copper active site	
1.14.99.56	Cu2+	enzyme is Cu(II) saturated with a 3fold molar excess of Cu(II)SO4 prior to assay	
1.14.99.56	Cu2+	the active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry	
1.14.99.56	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	
1.14.99.56	Cu2+	the reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose