Please use this identifier to cite or link to this item:
|Title:||Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude|
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jun 29, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.