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1.14.99.56
Cu2+
-
740210
,
745380
1.14.99.56
Cu2+
enzyme is Cu(II) saturated with a 3fold molar excess of Cu(II)SO4 prior to assay
744815
1.14.99.56
Cu2+
residue Tyr203 is placed approximately 15 A away from the copper active site
741041
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
745380
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
745387
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
745381
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