Journal
NATURE CHEMISTRY
Volume 6, Issue 3, Pages 236-241Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.1856
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Funding
- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the US Department of Energy [DE-FG02-07ER15865]
- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the US Department of Energy at Argonne National Laboratory [DE-AC02-06CH11357]
- Dreyfus Foundation Postdoctoral Program in Environmental Chemistry
- Ministry of Science and Technology of China [2009CB918500]
- National Natural Science Foundation of China [21173013, 11021463]
- Office of Basic Energy Sciences of the US Department of Energy [DE-AC02-06CH11357]
- U.S. Department of Energy (DOE) [DE-FG02-07ER15865] Funding Source: U.S. Department of Energy (DOE)
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Uranyl (UO22+), the predominant aerobic form of uranium, is present in the ocean at a concentration of similar to 3.2 parts per 10(9) (13.7 nM); however, the successful enrichment of uranyl from this vast resource has been limited by the high concentrations of metal ions of similar size and charge, which makes it difficult to design a binding motif that is selective for uranyl. Here we report the design and rational development of a uranyl-binding protein using a computational screening process in the initial search for potential uranyl-binding sites. The engineered protein is thermally stable and offers very high affinity and selectivity for uranyl with a K-d of 7.4 femtomolar (fM) and >10,000-fold selectivity over other metal ions. We also demonstrated that the uranyl-binding protein can repeatedly sequester 30-60% of the uranyl in synthetic sea water. The chemical strategy employed here may be applied to engineer other selective metal-binding proteins for biotechnology and remediation applications.
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