- V2O5 nanowires with an intrinsic peroxidase-like activity
- Advanced Functional Materials
- Volume | Issue number
- 21 | 3
- Pages (from-to)
- Document type
- Faculty of Science (FNWI)
- Van 't Hoff Institute for Molecular Sciences (HIMS)
V2O5 nanowires exhibit an intrinsic catalytic activity towards classical peroxidase substrates such as 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 3,3,5,5,-tetramethylbenzdine (TMB) in the presence of H2O2. These V2O5 nanowires show an optimum reactivity at a pH of 4.0 and the catalytic activity is dependent on the concentration. The Michaelis-Menten kinetics of the ABTS oxidation over these nanowires reveals a behavior similar to that of their natural vanadium-dependent haloperoxidase (V-HPO) counterparts. The V2O5 nanowires mediate the oxidation of ABTS in the presence of H2O2 with a turnover frequency (k(cat)) of 2.5 x 10(3) s(-1). The K-M values of the V2O5 nanowires for ABTS oxidation (0.4 mu M) and for H2O2 (2.9 mu M) at a pH of 4.0 are significantly smaller than those reported for horseradish peroxidases (HRP) and V-HPO indicating a higher affinity of the substrates for the V2O5 nanowire surface. Based on the kinetic parameters and similarity with vanadium-based complexes a mechanism is proposed where an intermediate metastable peroxo complex is formed as the first catalytic step. The nanostructured vanadium-based material can be re-used up to 10 times and retains its catalytic activity in a wide range of organic solvents (up to 90%) making it a promising mimic of peroxidase catalysts.
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