Please use this identifier to cite or link to this item: https://doi.org/10.1039/c2cc30901g
Title: Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude
Authors: New, S.Y.
Marshall, N.M.
Hor, T.S.A. 
Xue, F. 
Lu, 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

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

11
checked on May 19, 2018

WEB OF SCIENCETM
Citations

12
checked on Apr 2, 2018

Page view(s)

23
checked on May 18, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.