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Rationally tuning the reduction potential of a single cupredoxin beyond the natural range

Author

Listed:
  • Nicholas M. Marshall

    (University of Illinois, Urbana-Champaign, Illinois 61801, USA)

  • Dewain K. Garner

    (University of Illinois, Urbana-Champaign, Illinois 61801, USA)

  • Tiffany D. Wilson

    (University of Illinois, Urbana-Champaign, Illinois 61801, USA)

  • Yi-Gui Gao

    (University of Illinois, Urbana-Champaign, Illinois 61801, USA)

  • Howard Robinson

    (Brookhaven National Laboratory, Upton, New York 11973-5000, USA)

  • Mark J. Nilges

    (University of Illinois, Urbana-Champaign, Illinois 61801, USA)

  • Yi Lu

    (University of Illinois, Urbana-Champaign, Illinois 61801, USA)

Abstract

'Super' metalloproteins Many metalloproteins — proteins that contain metal atoms in their active sites — are crucial for biological reactions involving electron transfer. Marshall et al. now demonstrate that it is possible to tune the reduction potential of a single cupredoxin molecule — the arsenate reductase known as azurin — to well beyond the natural range. This is achieved by changing key amino acids near, or distal to, the metal binding site. The hope is that the lessons learned from this work, and future studies, could be used to design non-natural photosynthetic centres or artificial fuel cell catalysts for energy conversion.

Suggested Citation

  • Nicholas M. Marshall & Dewain K. Garner & Tiffany D. Wilson & Yi-Gui Gao & Howard Robinson & Mark J. Nilges & Yi Lu, 2009. "Rationally tuning the reduction potential of a single cupredoxin beyond the natural range," Nature, Nature, vol. 462(7269), pages 113-116, November.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7269:d:10.1038_nature08551
    DOI: 10.1038/nature08551
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