V2O5 Nanowires with an Intrinsic Peroxidase-Like Activity

Authors

  • Rute André,

    1. Institute for Inorganic Chemistry Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany
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  • Filipe Natálio,

    1. Institute for Inorganic Chemistry Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany
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  • Madalena Humanes,

    1. Center of Chemistry and Biochemistry Department of Chemistry and Biochemistry Faculty of Sciences University of Lisbon Building C8, Campo Grande 1749–016 Lisbon, Portugal
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  • Jana Leppin,

    1. Institute for Inorganic Chemistry Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany
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  • Katja Heinze,

    1. Institute for Inorganic Chemistry Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany
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  • Ron Wever,

    1. Van’t Hoff Institute for Molecular Sciences Universiteit van Amsterdam Nieuwe Achtergracht 129, 1018 WS Amsterdam, Holland
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  • H.-C. Schröder,

    1. Institute for Physiological Chemistry Dept. for Applied Molecular Genetics Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany
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  • Werner E. G. Müller,

    1. Institute for Physiological Chemistry Dept. for Applied Molecular Genetics Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany
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  • Wolfgang Tremel

    Corresponding author
    1. Institute for Inorganic Chemistry Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany
    • Institute for Inorganic Chemistry Johannes Gutenberg-University Duesbergweg 10–14, D–55099 Mainz, Germany.
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Abstract

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 (kcat) of 2.5 × 103 s−1. The KM values of the V2O5 nanowires for ABTS oxidation (0.4 μM) and for H2O2 (2.9 μM) 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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