The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system.
In anaerobic environments the first electron transfer in substrate-free P450cam is known to be thermodynamically unfavourable, but in the presence of dioxygen the reduction potential for the reaction shifts positively to make electron transfer thermodynamically favourable. Nevertheless a slower rate...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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1999
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| _version_ | 1826282968862162944 |
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| author | Honeychurch, M Hill, A Wong, L |
| author_facet | Honeychurch, M Hill, A Wong, L |
| author_sort | Honeychurch, M |
| collection | OXFORD |
| description | In anaerobic environments the first electron transfer in substrate-free P450cam is known to be thermodynamically unfavourable, but in the presence of dioxygen the reduction potential for the reaction shifts positively to make electron transfer thermodynamically favourable. Nevertheless a slower rate of electron transfer is observed in the substrate-free P450cam compared to substrate-bound P450cam. The ferric haem centre in substrate-free P450cam changes from six co-ordinate to five co-ordinate when reduced whereas in substrate-bound P450cam the iron centre remains five co-ordinate in both oxidation states. The slower rate of electron transfer in the substrate-free P450cam is therefore attributed to a larger reorganisation energy as predicted by Marcus theory. |
| first_indexed | 2024-03-07T00:51:51Z |
| format | Journal article |
| id | oxford-uuid:86acf500-2426-4cff-8245-12d0be0ee2bf |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:51:51Z |
| publishDate | 1999 |
| record_format | dspace |
| spelling | oxford-uuid:86acf500-2426-4cff-8245-12d0be0ee2bf2022-03-26T22:05:28ZThe thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:86acf500-2426-4cff-8245-12d0be0ee2bfEnglishSymplectic Elements at Oxford1999Honeychurch, MHill, AWong, LIn anaerobic environments the first electron transfer in substrate-free P450cam is known to be thermodynamically unfavourable, but in the presence of dioxygen the reduction potential for the reaction shifts positively to make electron transfer thermodynamically favourable. Nevertheless a slower rate of electron transfer is observed in the substrate-free P450cam compared to substrate-bound P450cam. The ferric haem centre in substrate-free P450cam changes from six co-ordinate to five co-ordinate when reduced whereas in substrate-bound P450cam the iron centre remains five co-ordinate in both oxidation states. The slower rate of electron transfer in the substrate-free P450cam is therefore attributed to a larger reorganisation energy as predicted by Marcus theory. |
| spellingShingle | Honeychurch, M Hill, A Wong, L The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system. |
| title | The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system. |
| title_full | The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system. |
| title_fullStr | The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system. |
| title_full_unstemmed | The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system. |
| title_short | The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system. |
| title_sort | thermodynamics and kinetics of electron transfer in the cytochrome p450cam enzyme system |
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