Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10267535 | Electrochemistry Communications | 2005 | 5 Pages |
Abstract
In aqueous buffer, haemoglobin and myoglobin undergo direct electron transfer at bare and didodecyldimethylammonium bromide modified pyrolytic graphite electrodes. On immersion of the protein modified electrodes in methanol and ethanol, both proteins displayed a faradaic response, with E°Ⲡdecreasing in comparison to the values obtained in aqueous buffer. Unlike haemoglobin, the E°Ⲡof myoglobin displayed a complex dependence on temperature, which was not observed with Hb, and displayed significant changes in ÎH°Ⲡand ÎS°â².
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Chemical Engineering (General)
Authors
Ekaterina V. Ivanova, Edmond Magner,