Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude

Siu Yee New, Nicholas M. Marshall, T. S.Andy Hor, Feng Xue, Yi Lu

Research output: Contribution to journalArticlepeer-review

Abstract

The same non-covalent interactions previously found to affect the redox potential (E m) of the mononuclear T1 Cu protein azurin (Az) are shown to also fine-tune the E m of the dinuclear Cu A center in the same Az protein scaffold. The effects of these mutations are in the same direction but with smaller magnitude in the Cu A site, due to dissipation of the effects by the dinuclear Cu A center.

Original languageEnglish (US)
Pages (from-to)4217-4219
Number of pages3
JournalChemical Communications
Volume48
Issue number35
DOIs
StatePublished - Apr 2 2012

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Fingerprint

Dive into the research topics of 'Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude'. Together they form a unique fingerprint.

Cite this