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Vanadium pentoxide nanoparticles mimic vanadium haloperoxidases and thwart biofilm formation


Marine biofouling—the colonization of small marine microorganisms on surfaces that are directly exposed to seawater, such as ships' hulls—is an expensive problem that is currently without an environmentally compatible solution1. Biofouling leads to increased hydrodynamic drag, which, in turn, causes increased fuel consumption and greenhouse gas emissions. Tributyltin-free antifouling coatings and paints1,2,3,4 based on metal complexes or biocides have been shown to efficiently prevent marine biofouling. However, these materials can damage5 the environment through metal leaching (for example, of copper and zinc)6 and bacteria resistance7. Here, we show that vanadium pentoxide nanowires act like naturally occurring vanadium haloperoxidases8 to prevent marine biofouling. In the presence of bromide ions and hydrogen peroxide, the nanowires catalyse the oxidation of bromide ions to hypobromous acid (HOBr). Singlet molecular oxygen (1O2) is formed and this exerts strong antibacterial activity, which prevents marine biofouling without being toxic to marine biota. Vanadium pentoxide nanowires have the potential to be an alternative approach to conventional anti-biofouling agents.

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Figure 1: Bactericidal properties of V2O5 nanowires.
Figure 2: TEM image of V2O5 nanowires and concentration dependence of their bromination activity.
Figure 3: Steady-state kinetics of the V2O5 nanowires at pH 8.3.
Figure 4: Representative digital images showing the influence of the catalytic activity of V2O5 nanowires on the growth of Gram-positive (S. aureus) and Gram-negative (E. coli) bacteria.
Figure 5: Application of V2O5 nanowires in paint with antibacterial/antifouling properties.
Figure 6: Effect of nanoparticles on biofouling in situ.


  1. 1

    Banerjee, I., Pangule, R. C. & Kane, R. S. Antifouling coatings: recent developments in the design of surfaces that prevent fouling by proteins, bacteria, and marine organisms. Adv. Mater. 23, 690–718 (2011).

    CAS  Article  Google Scholar 

  2. 2

    Messersmith, P. B. & Textor, M. Enzymes on nanotubes thwart fouling. Nature Nanotech. 2, 138–139 (2007).

    CAS  Article  Google Scholar 

  3. 3

    Chambers, L. D., Stokes, K. R., Walsh, F. C. & Wood, R. J. K. Modern approaches to marine antifouling coatings. Surf. Coat. Technol. 201, 3642–3652 (2006).

    CAS  Article  Google Scholar 

  4. 4

    Almeida, E., Diamantino, T. C. & Sousa, O. Marine paints: the particular case of antifouling paints. Prog. Org. Coat. 59, 2–20 (2007).

    CAS  Article  Google Scholar 

  5. 5

    Omae, I. General aspects of tin-free antifouling paints. Chem. Rev. 103, 3431–3448 (2003).

    CAS  Article  Google Scholar 

  6. 6

    Turley, P. A., Fenn, R. J. & Ritter, J. C. Pyrithiones as antifoulants: environmental chemistry and preliminary risk assessment. Biofouling 15, 175–182 (2000).

    CAS  Article  Google Scholar 

  7. 7

    Brozel, V. S., Pietersen, B. & Cloete, T. E. Resistance of bacterial cultures to nonoxidizing water-treatment bactericides by adaptation. Water Sci. Technol. 31, 169–175 (1995).

    CAS  Article  Google Scholar 

  8. 8

    Wever, R. & Hemrika, W. in Handbook of Metalloproteins (eds Messerschmidt, A., Huber, R., Poulos, T. & Wieghardt, K.) 1417–1428 (Wiley, 2001).

    Google Scholar 

  9. 9

    Rosenhahn, A., Schilp, S., Kreuzer, H. J. & Grunze, M. The role of ‘inert’ surface chemistry in marine biofouling prevention. Phys. Chem. Chem. Phys. 12, 4275–4286 (2010).

    CAS  Article  Google Scholar 

  10. 10

    Borchardt, S. A. et al. Reaction of acylated homoserine lactone bacterial signaling molecules with oxidized halogen antimicrobials. Appl. Environ. Microbiol. 67, 3174–3179 (2001).

    CAS  Article  Google Scholar 

  11. 11

    Wever, R., Tromp, M. G. M., Krenn, B. E., Marjani, A. & van Tol, M. Brominating activity of the seaweed Ascophyllum Nodosum: impact on the biosphere. Environ. Sci. Technol. 25, 446–449 (1991).

    CAS  Article  Google Scholar 

  12. 12

    Barnett, P., Hondmann, D., Simons, L. H., Ter Steeg, P. F. & Wever, R. Recombinant vanadium haloperoxidases and their uses. Patent WO/1995/027046 (1995).

  13. 13

    Wever, R., Dekker, H. L., Van Schijndel, J. W. P. M. & Vollenbroek, E. G. M. Antifouling Paint Containing Haloperoxidase and Method to Determine Halide. Patent WO/1995/027009 (1995).

  14. 14

    Weller, R. & Schrems, O. H2O2 in the marine troposphere and seawater of the Atlantic Ocean. Geophys. Res. Lett. 20, 125–128 (1993).

    CAS  Article  Google Scholar 

  15. 15

    Hasan, Z. et al. Laboratory evolved vanadium chloroperoxidase exhibits 100-fold higher halogenating activity at alkaline pH: catalytic effects from first and second coordination sphere mutations. J. Biol. Chem. 281, 9738–9744 (2006).

    CAS  Article  Google Scholar 

  16. 16

    Almeida, M. et al. Vanadium haloperoxidases from brown algae of the Laminariaceae Family. Phytochemistry 57, 633–642 (2001).

    CAS  Article  Google Scholar 

  17. 17

    Soedjak, H. S., Walker, J. V. & Butler, A. Inhibition and inactivation of vanadium bromoperoxidase by the substrate, hydrogen peroxide, and further mechanistic studies of vanadium bromoperoxidase. Biochemistry 34, 12689–12696 (1995).

    CAS  Article  Google Scholar 

  18. 18

    Crans, D. C., Smee, J. J., Gaidamauskas, E. & Yang, L. The chemistry and biochemistry of vanadium and the biological activities exerted by vanadium compounds. Chem. Rev. 104, 849–902 (2004).

    CAS  Article  Google Scholar 

  19. 19

    Mimoun, H. et al. Vanadium(V) peroxy complexes. New versatile biomimetic reagents for epoxidation of olefins and hydroxylation of alkanes and aromatic hydrocarbons. J. Am. Chem. Soc. 105, 3101–3110 (1983).

    CAS  Article  Google Scholar 

  20. 20

    De la Rosa, R. I., Clague, M. J. & Butler, A. A functional mimic of vanadium bromoperoxidase. J. Am. Chem. Soc. 114, 760–767 (1992).

    CAS  Article  Google Scholar 

  21. 21

    André, R. et al. V2O5 nanowires with an intrinsic peroxidase-like activity. Adv. Funct. Mater. 21, 501–509 (2011).

    Article  Google Scholar 

  22. 22

    De Boer, E. & Wever, R. The reaction mechanism of the novel vanadium bromoperoxidase. A steady-state kinetic analysis. J. Biol. Chem. 263, 12326–12332 (1988).

    CAS  Google Scholar 

  23. 23

    Butler, A. in Bioinorganic Catalysis 2nd edn (eds Reedijk, J. & Bouwman, E.) Ch. 5, 55–79 (Marcel Dekker, 1991).

    Google Scholar 

  24. 24

    Hemrika, W., Renirie, R., Dekker, H. L., Barnett, P. & Wever, R. From phosphatases to vanadium peroxidases: a similar architecture of the active site. Proc. Natl Acad. Sci. USA 94, 2145–2149 (1997).

    CAS  Article  Google Scholar 

  25. 25

    Shevelkova, A. N. & Ryabov, A. D. Irreversible inactivation of Caldariomyces fumago chloroperoxidase by hydrogen peroxide. IUBMB Life 39, 665–670 (1996).

    CAS  Article  Google Scholar 

  26. 26

    Butler, A., Clague, M. J. & Meister, G. E. Vanadium peroxide complexes. Chem. Rev. 94, 625–638 (1994).

    CAS  Article  Google Scholar 

  27. 27

    Colpas, G. J., Hamstra, B. J., Kampf, J. W. & Pecoraro, V. L. Functional models for vanadium haloperoxidase: reactivity and mechanism of halide oxidation. J. Am. Chem. Soc. 118, 3469–3478 (1996).

    CAS  Article  Google Scholar 

  28. 28

    De la Rosa, R. I., Clague, M. J. & Butler, A. A. Functional mimic of vanadium bromoperoxidase. J. Am. Chem. Soc. 114, 760–761 (1992).

    CAS  Article  Google Scholar 

  29. 29

    Ligtenbarg, A. G. J., Hage, R. & Feringa, B. L. Catalytic oxidations by vanadium complexes. Coord. Chem. Rev. 237, 89–101 (2003).

    CAS  Article  Google Scholar 

  30. 30

    Renirie, R. et al. Vanadium chloroperoxidase as a catalyst for hydrogen peroxide disproportionation to singlet oxygen in mildly acidic aqueous environment. Adv. Synth. Catal. 345, 849–858 (2003).

    CAS  Article  Google Scholar 

  31. 31

    Soedjak, H. S. & Butler, A. Mechanism of dioxygen formation catalyzed by vanadium-bromoperoxidase from Macrocystis pyrifera and Fucus distichus: steady state kinetic analysis and comparison to the mechanism of V-BrPO from Ascophyllum nodosum. Biochim. Biophys. Acta. 1079, 1–7 (1991).

    CAS  Article  Google Scholar 

  32. 32

    Butler, A. Acquisition and utilization of transition metal ions by marine organisms. Science 281, 207–210 (1998).

    CAS  Article  Google Scholar 

  33. 33

    Beers, R. F. & Sizer, I. W. Spectrophotometric methods for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195, 133–140 (1952).

    CAS  Google Scholar 

  34. 34

    Wang, D. & Sañudo-Wilhelmy, S. A. Development of an analytical protocol for the determination of V(IV) and V(V) in seawater: application to coastal environments. Mar. Chem. 112, 72–80 (2008).

    CAS  Article  Google Scholar 

  35. 35

    Sachs, L. Angewandte Statistik 242 (Springer, 1984).

    Book  Google Scholar 

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This research was supported by the European community through the project BIOMINTEC (PITN-GA-2008215507) and the BMBF center of Excellence BIOTEC Marin. The authors acknowledge partial support from the Center for Complex Matter (COMATT) at the University of Mainz.

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F.N., R.A. and A.F.H. carried out the experiments. R.W. and W.T. conceived the experiments. B.S. and K.P.J. contributed with the ICP-MS measurements. W.T. wrote the manuscript with contributions from F.N.

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Correspondence to Wolfgang Tremel.

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The authors declare no competing financial interests.

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Natalio, F., André, R., Hartog, A. et al. Vanadium pentoxide nanoparticles mimic vanadium haloperoxidases and thwart biofilm formation. Nature Nanotech 7, 530–535 (2012).

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