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 language | English (US) |
|---|---|
| Pages (from-to) | 4217-4219 |
| Number of pages | 3 |
| Journal | Chemical Communications |
| Volume | 48 |
| Issue number | 35 |
| DOIs | |
| State | Published - Apr 2 2012 |
ASJC Scopus subject areas
- Catalysis
- Electronic, Optical and Magnetic Materials
- Ceramics and Composites
- General Chemistry
- Surfaces, Coatings and Films
- Metals and Alloys
- Materials Chemistry
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