“…The binding energy (BE) at ∼934.48 and ∼954.39 eV of the Cu 2p spectrum in Figure D could be assigned to Cu 2p 3/2 and Cu 2p 1/2 of Cu(II), respectively. − The peaks at ∼932.47 and ∼952.43 eV could belong to Cu 2p 3/2 of Cu(I) and Cu 2p 1/2 of Cu(II), respectively. , The peaks at ∼944.22 and ∼941.68 eV were connected with Cu(II). , Additionally, the BE at ∼284.78, ∼285.80, and ∼287.97 eV in C 1s spectrum of His could be corresponded to CC/CC, CO, and CN, respectively. − Three peaks at ∼284.66, ∼285.60, and ∼287.46 eV in the C 1s spectrum of CHzyme could be assigned to CC/CC, CO, and CN, respectively (Figure E). − Meanwhile, two peaks at ∼530.67 and ∼531.42 eV in O 1s of His could be attributed to the CO bond and −OH. , Three peaks in O 1s of CHzyme at ∼530.35, ∼531.09, and ∼532.05 eV could be attributed to CuO, CO, and −OH, respectively, demonstrating the successful coordination between Cu and oxygen atoms (Figure F). − To demonstrate the coordination of Cu(II) and N atoms in His, the N 1s spectrum of CHzyme was further researched (Figure G). Two peaks at ∼400.23 and ∼398.26 eV in N 1s of His could be attributed to amino groups and the CN bond, respectively. , The BE of ∼400.28 and ∼398.39 eV of CHzyme could be assigned to amino groups and the CN bond in His, respectively. , The peak at ∼399.20 eV exhibited the existing Cu–N bonds, confirming the successful coordination between Cu and N atom in CHzyme . Meanwhile, Fourier transform infrared (FT-IR) spectroscopy was used to analyze the chemical bonding structure status of the prepared CHzyme (Figure H).…”