Rational design of a structural and functional nitric oxide reductase

Natasha Yeung, Ying-Wu Lin, Yi-Gui Gao, Xuan Zhao, Brandy S. Russell, Lanyu Lei, Kyle D. Miner, Howard Robinson and Yi Lu ()
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Natasha Yeung: Department of Chemistry,
Ying-Wu Lin: Department of Chemistry,
Yi-Gui Gao: George L. Clark X-Ray Facility and 3M Materials Laboratory,
Xuan Zhao: Department of Chemistry,
Brandy S. Russell: Department of Chemistry,
Lanyu Lei: Department of Chemistry,
Kyle D. Miner: University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA
Howard Robinson: Brookhaven National Laboratory, Upton, New York 11973, USA
Yi Lu: Department of Chemistry,

Nature, 2009, vol. 462, issue 7276, 1079-1082

Abstract: A nitric oxide reductase by design Considerable progress has been made in the design of proteins that mimic native proteins both structurally and functionally. Metalloproteins present more of a challenge owing to their complexity, but Yi Lu and colleagues now report the successful design of a structural and functional model of the metalloprotein nitric oxide reductase (NOR). An X-ray crystal structure of the designed protein confirms that it contains a haem/non-haem FeB centre very similar to that in the native protein, and also exhibits NOR activity.

Date: 2009
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DOI: 10.1038/nature08620

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