Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme?
The first electrochemical and infra-red data on the binding of cyanide to the isolated iron-molybdenum cofactor of nitrogenase, FeMoco, is described. It is shown that cyanide stabilises a hitherto unrecognised, low-spin, EPR-active (S= 1/2), superoxidised form of FeMoco, and we provide the first evi...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
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2004
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| _version_ | 1797059036663775232 |
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| author | Pickett, C Vincent, K Ibrahim, S Gormal, C Smith, B Fairhurst, SA Best, S |
| author_facet | Pickett, C Vincent, K Ibrahim, S Gormal, C Smith, B Fairhurst, SA Best, S |
| author_sort | Pickett, C |
| collection | OXFORD |
| description | The first electrochemical and infra-red data on the binding of cyanide to the isolated iron-molybdenum cofactor of nitrogenase, FeMoco, is described. It is shown that cyanide stabilises a hitherto unrecognised, low-spin, EPR-active (S= 1/2), superoxidised form of FeMoco, and we provide the first evidence that carbon monoxide and cyanide bind synergically to the oxidised and semireduced states of the isolated cofactor, states which are unreactive to carbon monoxide alone. |
| first_indexed | 2024-03-06T19:58:34Z |
| format | Journal article |
| id | oxford-uuid:267c0577-462b-4d58-8629-e2a34344eb3f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:58:34Z |
| publishDate | 2004 |
| record_format | dspace |
| spelling | oxford-uuid:267c0577-462b-4d58-8629-e2a34344eb3f2022-03-26T12:01:15ZSynergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme?Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:267c0577-462b-4d58-8629-e2a34344eb3fEnglishSymplectic Elements at Oxford2004Pickett, CVincent, KIbrahim, SGormal, CSmith, BFairhurst, SABest, SThe first electrochemical and infra-red data on the binding of cyanide to the isolated iron-molybdenum cofactor of nitrogenase, FeMoco, is described. It is shown that cyanide stabilises a hitherto unrecognised, low-spin, EPR-active (S= 1/2), superoxidised form of FeMoco, and we provide the first evidence that carbon monoxide and cyanide bind synergically to the oxidised and semireduced states of the isolated cofactor, states which are unreactive to carbon monoxide alone. |
| spellingShingle | Pickett, C Vincent, K Ibrahim, S Gormal, C Smith, B Fairhurst, SA Best, S Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme? |
| title | Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme? |
| title_full | Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme? |
| title_fullStr | Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme? |
| title_full_unstemmed | Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme? |
| title_short | Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme? |
| title_sort | synergic binding of carbon monoxide and cyanide to the femo cofactor of nitrogenase relic chemistry of an ancient enzyme |
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