Please use this identifier to cite or link to this item:
https://doi.org/10.1039/c2cc30901g
DC Field | Value | |
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dc.title | Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude | |
dc.contributor.author | New, S.Y. | |
dc.contributor.author | Marshall, N.M. | |
dc.contributor.author | Hor, T.S.A. | |
dc.contributor.author | Xue, F. | |
dc.contributor.author | Lu, Y. | |
dc.date.accessioned | 2014-10-16T08:39:02Z | |
dc.date.available | 2014-10-16T08:39:02Z | |
dc.date.issued | 2012-05-04 | |
dc.identifier.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 | |
dc.identifier.issn | 13597345 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/94697 | |
dc.description.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. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1039/c2cc30901g | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | CHEMISTRY | |
dc.description.doi | 10.1039/c2cc30901g | |
dc.description.sourcetitle | Chemical Communications | |
dc.description.volume | 48 | |
dc.description.issue | 35 | |
dc.description.page | 4217-4219 | |
dc.description.coden | CHCOF | |
dc.identifier.isiut | 000302309100020 | |
Appears in Collections: | Staff Publications |
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