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

Nicholas M. Marshall, Dewain K. Garner, Tiffany D. Wilson, Yi-Gui Gao, Howard Robinson, Mark J. Nilges and Yi Lu ()
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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

Nature, 2009, vol. 462, issue 7269, 113-116

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.

Date: 2009
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DOI: 10.1038/nature08551

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