Rational Design of Protein Cages for Alternative Enzymatic Functions

Nicholas M. Marshall, Kyle D. Miner, Tiffany D. Wilson, Yi Lu

Research output: Chapter in Book/Report/Conference proceedingChapter


This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.

Original languageEnglish (US)
Title of host publicationCoordination Chemistry in Protein Cages
Subtitle of host publicationPrinciples, Design, and Applications
PublisherJohn Wiley and Sons
Number of pages37
ISBN (Print)9781118078570
StatePublished - Apr 2 2013


  • Alternative enzymatic functions
  • Cupredoxin proteins
  • Heme-based enzymes
  • Metalloenzyme
  • Protein cage

ASJC Scopus subject areas

  • Chemistry(all)

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    Marshall, N. M., Miner, K. D., Wilson, T. D., & Lu, Y. (2013). Rational Design of Protein Cages for Alternative Enzymatic Functions. In Coordination Chemistry in Protein Cages: Principles, Design, and Applications (pp. 111-147). John Wiley and Sons. https://doi.org/10.1002/9781118571811.ch5