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Issue 35, 2012
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Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude

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Abstract

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

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

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Article information


Submitted
08 Feb 2012
Accepted
28 Feb 2012
First published
29 Feb 2012

Chem. Commun., 2012,48, 4217-4219
Article type
Communication

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

S. Y. New, N. M. Marshall, T. S. A. Hor, F. Xue and Y. Lu, Chem. Commun., 2012, 48, 4217
DOI: 10.1039/C2CC30901G

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