Fig. 4: Detection of enzyme-mimicking activity and steady-state kinetics of MxV2O5·nH2O. | Nature Communications

Fig. 4: Detection of enzyme-mimicking activity and steady-state kinetics of MxV2O5·nH2O.

From: Biomimetic synergistic effect of redox site and Lewis acid for construction of efficient artificial enzyme

Fig. 4

A UV-vis absorption spectra of oxTMB in the presence of H2O2 with MxV2O5·nH2O, V2O5 powder, V2O5 nanobelt, respectively. B The generation of ·OH testified by ESR spectra of MxV2O5·nH2O, V2O5 powder, V2O5 nanobelt in the presence of H2O2. C Absorbance of oxTMB in the presence of H2O2 and MxV2O5·nH2O/V2O5 nanobelt after adding isopropanol. n  =  3 experimental replicates. Data are presented as mean values  ±  SD. The data were analyzed by using a one-sided unpaired t-test. ****P < 0.0001. D Time-dependent absorbance of oxTMB (a), reaction rate (b) with different concentrations of TMB and fixed concentrations of MgVO/H2O2, and the corresponding double reciprocal (Lineweaver-Burk) plots (inset). E Time-dependent absorbance of oxTMB (a), reaction rate (b) with different concentrations of H2O2 and fixed concentrations of MgVO/TMB, and the corresponding double reciprocal (Lineweaver-Burk) plots (inset). n  =  3 experimental replicates (D, E (b)). Data are presented as mean values  ±  SD (D, E (b)). Vmax and Km values of MxV2O5·nH2O/V2O5 nanobelt towards to TMB (F) and (G) H2O2. H The comparison of the TON and Vmax values of MxV2O5·nH2O with other recently reported catalysts. I The comparison of the relative catalytic activity of MxV2O5·nH2O and synthesized peroxidase mimics. n  =  3 experimental replicates. Data are presented as mean values  ±  SD. Data were analyzed by one-way ANOVA with Turkey’s multiple comparisons test, ns represented no statistical difference, ****P < 0.0001.

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