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Enzymatic Synthesis of Platinum Nanoparticles: Prokaryote and Eukaryote Systems

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Metal Nanoparticles in Microbiology

Abstract

Efforts to discover an efficient yet environmentally friendly mode of metal nanoparticle (NP) synthesis are increasing rapidly and a “green” route that avoids the high costs, toxic wastes and complicated protocols associated with chemical synthesis methods is therefore highly sought after. A biologically based protocol would provide control over the mechanism of formation of nanoparticles by manipulating the experimental conditions of the system. Since the properties of these particles are highly dependant on their morphology, this control would have significant industrial advantages with regards to tailoring specific properties of the nanoparticles produced. Biological routes involving prokaryote/eukaryote systems provide great advantages over traditional methods, as they have the potential to be a cost efficient, simple, environmentally friendly and an efficient form of metal NP synthesis, which could produce NPs that are superior in quality and value. Both prokaryotic and eukaryotic organisms including bacteria, fungi, actinomycetes and yeasts synthesise biogenic geometric metal particles, in the nanometre range via an active and/or passive bioreductive process, when exposed to metal chloride solutions. Sulfate-reducing bacteria (SRB) (prokaryote) and the fungus Fusarium (eukaryote) have been cited in the literature as excellent models for metal bioremediation and it has been suggested that one or more hydrogenase/reductase enzymes are responsible. The sulfate-reducing consortium was shown to possess an aerobic mechanism for Pt(IV) reduction which, though different from the anaerobic bioreductive mechanism previously identified in literature, did not require an exogenous electron donor. It is shown that the Pt(IV) ion becomes reduced to Pt(0) via a two-cycle mechanism involving Pt(II) as the intermediate. Further investigation elucidated the reduction of Pt(IV) to Pt(II) to be dependant on a novel Pt(IV) cytoplasmic dehydrogenase while the reduction of Pt(II) to Pt(0) occurred by means of a periplasmic hydrogenase. SRB cells, under the same conditions as above, but challenged with a solution of Pt(II) exhibited a colour change from yellow to dark brown indicating Pt(0) nanoparticle formation while the SRB cells that had been incubated in the presence of 5 mM Cu(II) [inhibitor of periplasmic but not cytoplasmic hydrogenases] gave a barely perceptible colour change. A mechanism for the bioreduction of H2PtCl6 and PtCI2 into platinum nanoparticles by a hydrogenase enzyme from Fusarium oxysporum is also proposed. Octahedral H2PtCl6 is too large to fit into the active region of the enzyme and, under conditions optimum for nanoparticle formation (pH 9, 65°C), undergoes a two-electron reduction to PtCl2 on the molecular surface of the enzyme. This smaller molecule is transported through hydrophobic channels within the enzyme to the active region where, under conditions optimal for hydrogenase activity (pH 7.5, 38°C), it undergoes a second two-electron reduction to Pt(0). H2PtCl6 was unreactive at pH 7.5, 38°C; PtCl2 was unreactive at pH 9, 65°C. Transmission electron microscopy and energy dispersive X-ray analyses indicated that Pt was being precipitated in the periplasm, a major area of hydrogenase activity in the cells. The nanoparticles produced by the bioreduction of PtCl2 were distinctly large rectangular and triangular to those produced from H2PtCl6 which were, predominantly, circular, monodisperse and varying in size. Nanoparticles produced by the hydrogenase at pH 9, 65°C were circular, triangular, pentagonal and hexagonal, often appearing as nanoplates, over a wide size distribution with the majority of them being about 40–60 nm. These nanoplates appeared to be stacked close to, or on top of, each other as a result of an overlap in nucleation times and subsequent attachment of the nanoparticles resulting in aggregation. These results indicated that in addition to pH and temperature, the oxidation state of the platinum salt played an important role in the mechanism and formation of the nanoparticles though the size and shape of the particles were uncontrollable.

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Authors and Affiliations

  1. Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, 94, Grahamstown, 6140, South Africa

    Chris Whiteley, Yageshni Govender & Tamsyn Riddin

  2. Department of Biotechnology, Sant Gadge Baba University, Amravati, Maharashtra, India

    Mahendra Rai

Authors
  1. Chris Whiteley
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  2. Yageshni Govender
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  3. Tamsyn Riddin
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  4. Mahendra Rai
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Correspondence to Chris Whiteley .

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Editors and Affiliations

  1. , Dept. Biotechnology, SGB Amravati University, Amravati, 444602, Maharashtra, India

    Mahendra Rai

  2. Instituto de Quimica, Lab. Biological Chemistry, Universidade Estadual de Campinas, Campinas, São Paulo, Brazil

    Nelson Duran

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Whiteley, C., Govender, Y., Riddin, T., Rai, M. (2011). Enzymatic Synthesis of Platinum Nanoparticles: Prokaryote and Eukaryote Systems. In: Rai, M., Duran, N. (eds) Metal Nanoparticles in Microbiology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-18312-6_5

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