Publications
Detailed Information
Symmetry-Adapted Synthesis of Dicopper Oxidases with Divergent Dioxygen Reactivity
Cited 5 time in
Web of Science
Cited 6 time in Scopus
- Authors
- Issue Date
- 2022-08
- Publisher
- American Chemical Society
- Citation
- Inorganic Chemistry, Vol.61 No.31, pp.12433-12441
- Abstract
- Artificial metalloenzymes have fed our understanding of how inorganic reactivities emerge, evolve, and diversify in protein environments. Herein, we created dinuclear copper oxidases by genetically encoding a metal-ligating unnatural amino acid (bpy-Ala) per protomer in the vicinity of the innate C2 rotational axis of a homo-oligomeric protein. The inherent protein symmetry allows the precise multiplication and placement of two Cu(bpy) species. Depending on the location of bpy-Ala, the tailor-made metalloenzymes exhibited electronically uncoupled or coupled dicopper sites. Consequently, they displayed various reactivities with dioxygen associated with multiple protons and electrons, illustrating a diverse chemical repertoire of artificial copper-dependent enzymes.
- ISSN
- 0020-1669
- Files in This Item:
- There are no files associated with this item.
- Appears in Collections:
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.