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|Title:||Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude||Authors:||New, S.Y.
|Issue Date:||4-May-2012||Citation:||New, S.Y., Marshall, N.M., Hor, T.S.A., Xue, F., Lu, Y. (2012-05-04). Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude. Chemical Communications 48 (35) : 4217-4219. ScholarBank@NUS Repository. https://doi.org/10.1039/c2cc30901g||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. © 2012 The Royal Society of Chemistry.||Source Title:||Chemical Communications||URI:||http://scholarbank.nus.edu.sg/handle/10635/94697||ISSN:||13597345||DOI:||10.1039/c2cc30901g|
|Appears in Collections:||Staff Publications|
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