Constructing manmade enzymes for oxygen activation

Craig T. Armstrong, Daniel W. Watkins, J. L. Ross Anderson*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

18 Citations (Scopus)

Abstract

Natural oxygenases catalyse the insertion of oxygen into an impressive array of organic substrates with exquisite efficiency, specificity and power unparalleled by current biomimetic catalysts. However, their true potential to provide tailor-made oxygenation catalysts remains largely untapped, perhaps a consequence of the evolutionary complexity imprinted into their three-dimensional structures through millennia of exposure to parallel selective pressures. In this perspective we describe how we may take inspiration from natural enzymes to design manmade oxygenase enzymes free from such complexity. We explore the differing chemistries accessed by natural oxygenases and outline a stepwise methodology whereby functional elements key to oxygenase catalysis are assembled within artificially designed protein scaffolds.

Original languageEnglish
Pages (from-to)3136-3150
Number of pages15
JournalDalton Transactions
Volume42
Issue number9
DOIs
Publication statusPublished - 2013

Keywords

  • DE-NOVO DESIGN
  • HELICAL COILED-COILS
  • MEDIATED ELECTRON-TRANSFER
  • HEME-CONTAINING OXYGENASES
  • LABORATORY EVOLUTION
  • PROTEIN-DESIGN
  • COMBINATORIAL LIBRARY
  • SUBSTRATE-SPECIFICITY
  • PEROXIDASE-ACTIVITY
  • DIRECTED EVOLUTION

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