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Updated: May 23, 2026

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
Published on: November 26, 2014
Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude
Siu Yee New1, Nicholas M Marshall, T S Andy Hor
1Department of Chemistry, National University of Singapore, 3 Science Drive 3, Singapore 117543.
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.
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