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Chem Commun (Camb). 2012 May 4;48(35):4217-9. doi: 10.1039/c2cc30901g. Epub 2012 Mar 22.

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

Author information

1
Department 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.

PMID:
22441412
DOI:
10.1039/c2cc30901g
[Indexed for MEDLINE]

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