Fig. 3: Oxidase-mimicking activities of metal single-atom catalysts.
From: Kinetically restrained oxygen reduction to hydrogen peroxide with nearly 100% selectivity
a Schematic of flavoenzymes catalyzing the dehydrogenation of various substrates and O2 reduction to H2O2. b Active site of the alcohol oxidase from Pichia pastoris. c pH-dependent H2O2 production rate in the Rh1/NC-catalyzed benzyl alcohol oxidation reaction. d CV curves of Rh1/NC in a N2-saturated 0.1 M NaOH + 50 mM benzyl alcohol solution and in N2-saturated and O2-saturated 0.1 M NaOH solutions with a scan rate of 100 mV s−1. e Relative H2O2 production rate in the benzyl alcohol oxidation reaction with different catalysts. f H2O2 concentrations after the reaction of Rh1/NC (20 μg mL−1) and different substrates (10 mM, 0.1 mM for NADH and cysteine) for 5 min. Data are presented as mean values (SD). (The error bar represents the standard deviation of 3 independent measurements).
