Possible peroxidase active site environment in amyloidogenic proteins: Native monomer or misfolded-oligomer; which one is susceptible to the enzymatic activity, with contribution of heme?

Design and application of histidine-functionalized ZnCr-LDH nanozyme for promoting bacteria-infected wound healing

“…His residue in the horseradish peroxidase (HRP) enzyme active site prepares an electronic local in natural enzymes active site to increase the production of hydroxyl radicals. 30,31 In addition, the distal histidine amino acid of HRP activates H 2 O 2 molecules, binds them to the activated site's surface, and accelerates ROS production. 32 Herein, His provides the possibility of an effective catalytic performance through forming a hydrogen bond between the deprotonated N atom of its imidazole ring and the H atom of H 2 O 2 thereby, the activation of H 2 O 2 .…”