Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface
We report here the influence of chemical denaturation of haemoglobin on its electrochemical behaviour at the polarised liquid|liquid interface. Denaturation with urea resulted in a modification of the haemoglobin electrochemical behaviour, with the disappearance of the forward transfer peak and a de...
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| Format: | Journal Article |
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Elsevier
2010
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| Online Access: | http://hdl.handle.net/20.500.11937/21677 |
| _version_ | 1848750656892960768 |
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| author | Herzog, G. Eichelmann-Daly, P. Arrigan, Damien |
| author_facet | Herzog, G. Eichelmann-Daly, P. Arrigan, Damien |
| author_sort | Herzog, G. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | We report here the influence of chemical denaturation of haemoglobin on its electrochemical behaviour at the polarised liquid|liquid interface. Denaturation with urea resulted in a modification of the haemoglobin electrochemical behaviour, with the disappearance of the forward transfer peak and a decrease of the reverse peak current. Although the reverse peak current increased linearly with the concentration of denatured haemoglobin in the aqueous phase, the slope of the current-concentration plot was three times lower than that for native haemoglobin over the 0.1-1 μM concentration range. These results indicate the sensitivity of electrochemistry at liquid|liquid interfaces to protein tertiary structure. |
| first_indexed | 2025-11-14T07:40:18Z |
| format | Journal Article |
| id | curtin-20.500.11937-21677 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T07:40:18Z |
| publishDate | 2010 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-216772017-09-13T15:59:26Z Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface Herzog, G. Eichelmann-Daly, P. Arrigan, Damien Liquid|liquid interface Denaturation Voltammetry Haemoglobin Protein We report here the influence of chemical denaturation of haemoglobin on its electrochemical behaviour at the polarised liquid|liquid interface. Denaturation with urea resulted in a modification of the haemoglobin electrochemical behaviour, with the disappearance of the forward transfer peak and a decrease of the reverse peak current. Although the reverse peak current increased linearly with the concentration of denatured haemoglobin in the aqueous phase, the slope of the current-concentration plot was three times lower than that for native haemoglobin over the 0.1-1 μM concentration range. These results indicate the sensitivity of electrochemistry at liquid|liquid interfaces to protein tertiary structure. 2010 Journal Article http://hdl.handle.net/20.500.11937/21677 10.1016/j.elecom.2009.12.020 Elsevier fulltext |
| spellingShingle | Liquid|liquid interface Denaturation Voltammetry Haemoglobin Protein Herzog, G. Eichelmann-Daly, P. Arrigan, Damien Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface |
| title | Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface |
| title_full | Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface |
| title_fullStr | Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface |
| title_full_unstemmed | Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface |
| title_short | Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface |
| title_sort | electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface |
| topic | Liquid|liquid interface Denaturation Voltammetry Haemoglobin Protein |
| url | http://hdl.handle.net/20.500.11937/21677 |