1.14.99.54 Cu2+ - 735491, 739799, 740210, 745380 1.14.99.54 Cu2+ 1 mol of copper per mol of proein 739773 1.14.99.54 Cu2+ 1 mol of copper per mol of protein 739773 1.14.99.54 Cu2+ Cu(II) saturation of enzyme prior to assay 740400 1.14.99.54 Cu2+ CuII oxidation state 739859 1.14.99.54 Cu2+ EDTA-inhibited enzyme can be reactivated by 20 mM Cu2+ within 1 h 744633 1.14.99.54 Cu2+ enzyme is Cu(II) saturated with a 3fold molar excess of Cu(II)SO4 prior to assay 744815 1.14.99.54 Cu2+ presence of 1 copper atom per protein molecule 745847 1.14.99.54 Cu2+ strictly conserved copper-binding site which consists of two histidines (one at N-terminal position) and one tyrosine 735822 1.14.99.54 Cu2+ the active catalyst is Cu(II)-oxyl 741334 1.14.99.54 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 1.14.99.54 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 1.14.99.54 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 736485 1.14.99.54 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 741336 1.14.99.54 Cu2+ the copper site of CelS2 is similar to that of chitin-active LPMO10s. Dissociation constant is 31 nM 741336 1.14.99.54 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 745374 1.14.99.54 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 1.14.99.54 Cu2+ type II copper center, which exhibits a hexacoordination 740707