4.8 Review

Expanding the utility of proteins as platforms for coordination chemistry

期刊

COORDINATION CHEMISTRY REVIEWS
卷 255, 期 7-8, 页码 790-803

出版社

ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2010.10.010

关键词

Bioinorganic chemistry; Metal-protein interactions; Self-assembly; Protein-protein interactions; X-ray crystallography; Protein design

资金

  1. NSF [CHE-0908115]
  2. DOE BES [DE-FG02-10ER46677]
  3. Arnold and Mabel Beckman Foundation
  4. Sloan Foundation
  5. Hellman Family Fund
  6. UCSD
  7. Direct For Mathematical & Physical Scien
  8. Division Of Chemistry [0908115] Funding Source: National Science Foundation

向作者/读者索取更多资源

Whether for constructing advanced materials and complex biological devices or for building sophisticated coordination complexes with diverse metal-based functions, proteins are nature's favorite building blocks. Yet, our ability to control the assembly of proteins or to use them as ligand platforms for inorganic chemistry has been somewhat limited. In this review, we highlight our work from the past four years, which has aimed to exploit the utility of a protein scaffold in both regards. First, by considering proteins as simple ligand platforms and controlling the metal coordination chemistry on their surfaces, we show how their self-assembly can be readily dictated by metal binding. Second, we show how metal-mediated protein self-assembly leads to novel metal centers buried within protein interfaces. While on one hand our studies have pointed out the challenges of using proteins as ligands, they have also revealed how the extensive, chemically-rich protein surfaces can be exploited to form a network of covalent and non-covalent interactions around interfacial metal centers, providing a powerful handle to control their coordination chemistry. (C) 2010 Elsevier B.V. All rights reserved.

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