Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules.
Electrochemical reduction of H2O2 at pyrolytic graphite disc electrodes of radius 2.5 mm occurs at readily accessible potentials (600 mV versus the standard hydrogen electrode) in the presence of yeast cytochrome c peroxidase. Introduction of the enzyme into the electrolyte solution initiates large...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1993
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| _version_ | 1826299691455741952 |
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| author | Armstrong, F Bond, A Büchi, F Hamnett, A Hill, H Lannon, A Lettington, O Zoski, C |
| author_facet | Armstrong, F Bond, A Büchi, F Hamnett, A Hill, H Lannon, A Lettington, O Zoski, C |
| author_sort | Armstrong, F |
| collection | OXFORD |
| description | Electrochemical reduction of H2O2 at pyrolytic graphite disc electrodes of radius 2.5 mm occurs at readily accessible potentials (600 mV versus the standard hydrogen electrode) in the presence of yeast cytochrome c peroxidase. Introduction of the enzyme into the electrolyte solution initiates large changes in the ellipsometric angles measured for the electrode-solution interface, consistent with time-dependent enzyme adsorption. This process may be correlated with changes in electrochemical activity. Over the same time course, linear-sweep voltammograms are characterized by a transition from a sigmoidal to a peak-type waveform. It is proposed that the time-dependent behaviour may be rationalized by use of a microscopic model for substrate mass transport, in which the two-electron reduction of peroxide occurs at electrocatalytic sites consisting of adsorbed enzyme molecules. A voltammetric theory based on treating the adsorbed redox enzymes as an expanding array of microelectrodes is in excellent agreement with experiment. |
| first_indexed | 2024-03-07T05:05:48Z |
| format | Journal article |
| id | oxford-uuid:d9df2d2b-2e69-4627-8455-8a2110057e31 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:05:48Z |
| publishDate | 1993 |
| record_format | dspace |
| spelling | oxford-uuid:d9df2d2b-2e69-4627-8455-8a2110057e312022-03-27T08:59:07ZElectrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d9df2d2b-2e69-4627-8455-8a2110057e31EnglishSymplectic Elements at Oxford1993Armstrong, FBond, ABüchi, FHamnett, AHill, HLannon, ALettington, OZoski, CElectrochemical reduction of H2O2 at pyrolytic graphite disc electrodes of radius 2.5 mm occurs at readily accessible potentials (600 mV versus the standard hydrogen electrode) in the presence of yeast cytochrome c peroxidase. Introduction of the enzyme into the electrolyte solution initiates large changes in the ellipsometric angles measured for the electrode-solution interface, consistent with time-dependent enzyme adsorption. This process may be correlated with changes in electrochemical activity. Over the same time course, linear-sweep voltammograms are characterized by a transition from a sigmoidal to a peak-type waveform. It is proposed that the time-dependent behaviour may be rationalized by use of a microscopic model for substrate mass transport, in which the two-electron reduction of peroxide occurs at electrocatalytic sites consisting of adsorbed enzyme molecules. A voltammetric theory based on treating the adsorbed redox enzymes as an expanding array of microelectrodes is in excellent agreement with experiment. |
| spellingShingle | Armstrong, F Bond, A Büchi, F Hamnett, A Hill, H Lannon, A Lettington, O Zoski, C Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. |
| title | Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. |
| title_full | Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. |
| title_fullStr | Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. |
| title_full_unstemmed | Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. |
| title_short | Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. |
| title_sort | electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase a description based on a microelectrode array model for adsorbed enzyme molecules |
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