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Results 1 - 6 of 6
EC Number Metals/Ions Commentary Reference
Show all pathways known for 1.14.99.56Display the reaction diagram Show all sequences 1.14.99.56Cu2+ - 740210, 745380
Show all pathways known for 1.14.99.56Display the reaction diagram Show all sequences 1.14.99.56Cu2+ enzyme is Cu(II) saturated with a 3fold molar excess of Cu(II)SO4 prior to assay 744815
Show all pathways known for 1.14.99.56Display the reaction diagram Show all sequences 1.14.99.56Cu2+ residue Tyr203 is placed approximately 15 A away from the copper active site 741041
Show all pathways known for 1.14.99.56Display the reaction diagram Show all sequences 1.14.99.56Cu2+ the active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry 745380
Show all pathways known for 1.14.99.56Display the reaction diagram Show all sequences 1.14.99.56Cu2+ 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
Show all pathways known for 1.14.99.56Display the reaction diagram Show all sequences 1.14.99.56Cu2+ the reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose 745381
Results 1 - 6 of 6