Metalloprotein Design

Y. Lu, S. Chakraborty, K. D. Miner, T. D. Wilson, A. Mukherjee, Y. Yu, J. Liu, N. M. Marshall

Research output: Chapter in Book/Report/Conference proceedingChapter


Metalloproteins catalyze numerous biological reactions ranging from photosynthesis, respiration, nitrogen fixation to signal transduction and complex chemical reactions. It is thus not surprising that metalloproteins account for almost one-half of the total number of proteins in nature. A considerable effort has been directed toward understanding the structure-function relationships using native proteins. However, it is an ultimate challenge to design metalloproteins using only the minimal features required to reproduce their functionalities as well as confer them with novel and unprecedented functionalities learned from the design process. In this chapter, we review some recent successes in the field of metalloprotein design using either de novo designed or native protein scaffolds. Furthermore, metalloprotein design employing unnatural amino acids or non-native cofactor are summarized. Finally, methodologies employing rational design, combinatorial selection, or both methods are also discussed.

Original languageEnglish (US)
Title of host publicationComprehensive Inorganic Chemistry II (Second Edition)
Subtitle of host publicationFrom Elements to Applications
PublisherElsevier Ltd
Number of pages29
ISBN (Print)9780080965291
StatePublished - Aug 1 2013


  • Coiled coils
  • Combinatorial protein design
  • Cupredoxins
  • De novo design
  • Electron transfer
  • Expressed protein ligation
  • Helical bundles
  • Heme protein
  • Heme-copper oxidase
  • Myoglobin
  • Native chemical ligation
  • Nitric oxide reductase
  • Non-native cofactors
  • Redesign of proteins
  • Unnatural amino acids
  • Zinc metalloproteins

ASJC Scopus subject areas

  • Chemistry(all)

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