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On the enzymatic formation of platinum nanoparticles

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Abstract

A dimeric hydrogenase enzyme (44.5 and 39.4 kDa sub units) was isolated in a 39.5% yield from the fungus Fusarium oxysporum and purified 4.64-fold by ion exchange chromatography on Sephacryl S-200. Characterisation of the enzyme afforded pH and temperature optima of 7.5 and 38 °C, respectively, a half-life stability of 36 min and a V max and K m of 3.57 nmol min−1 mL−1 and 2.25 mM, respectively. This enzyme was inhibited (non-competitively) by hydrogen hexachloroplatinic acid (H2PtCl6) at 1 or 2 mM with a K i value of 118 μM. Incubation of the platinum salt with the pure enzyme under an atmosphere of hydrogen and optimum enzyme conditions (pH 7.5, 38 °C) afforded <10% bioreduction after 8 h while at conditions suitable for platinum nanoparticle formation (pH 9, 65 °C) over 90% reduction took place after the same length of time. Cell-free extract from the fungal isolates produced nearly 90% bioreduction of the platinum salt under both pH and temperature conditions. The bioreduction of the platinum salt by a hydrogenase enzyme takes place by a passive process and not an active one as previously understood.

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Acknowledgements

Financial assistance for YG and TR from MINTEK (South Africa) is gratefully appreciated

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Authors and Affiliations

  1. Department of Biochemistry, Microbiology & Biotechnology, Rhodes University, PO Box 94, 6140, Grahamstown, South Africa

    Y. Govender, T. L. Riddin & C. G. Whiteley

  2. MINTEK, Private Bag X3015, 2125, Randburg, South Africa

    M. Gericke

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  1. Y. Govender
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  2. T. L. Riddin
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  3. M. Gericke
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  4. C. G. Whiteley
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Correspondence to C. G. Whiteley.

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Govender, Y., Riddin, T.L., Gericke, M. et al. On the enzymatic formation of platinum nanoparticles. J Nanopart Res 12, 261–271 (2010). https://doi.org/10.1007/s11051-009-9604-3

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  • DOI: https://doi.org/10.1007/s11051-009-9604-3

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