Voltammetry of a "protein on a rope".
A periplasmic electron-transfer protein, cytochrome c(555)(m) from Aquifex aeolicus contains a 62-residue N-terminal extension by which it is anchored to the membrane--most probably via a thioester bond to its N-terminal cysteine. This linker can act as a "rope" to tether the protein close...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2003
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| _version_ | 1826295342203666432 |
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| author | Baymann, F Barlow, N Aubert, C Schoepp-Cothenet, B Leroy, G Armstrong, F |
| author_facet | Baymann, F Barlow, N Aubert, C Schoepp-Cothenet, B Leroy, G Armstrong, F |
| author_sort | Baymann, F |
| collection | OXFORD |
| description | A periplasmic electron-transfer protein, cytochrome c(555)(m) from Aquifex aeolicus contains a 62-residue N-terminal extension by which it is anchored to the membrane--most probably via a thioester bond to its N-terminal cysteine. This linker can act as a "rope" to tether the protein close to its reaction partners. Mimicking this principle, a recombinant cytochrome c(555)(m), expressed in Escherichia coli, has been attached covalently to a gold electrode modified with 6-mercaptohexan-1-ol. The "tethered" cytochrome c(555)(m) displays remarkably fast electron-transfer kinetics, with an electrochemical exchange rate constant k(0) of 1.4 x 10(4) s(-1). The results show that fast electron transfer is associated with weak interactions: importantly, the tethered cytochrome can explore many different orientations without escaping into solution. |
| first_indexed | 2024-03-07T03:59:33Z |
| format | Journal article |
| id | oxford-uuid:c4113e3b-8ebb-47a5-9822-bf4422f1a9b8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:59:33Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:c4113e3b-8ebb-47a5-9822-bf4422f1a9b82022-03-27T06:20:52ZVoltammetry of a "protein on a rope".Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c4113e3b-8ebb-47a5-9822-bf4422f1a9b8EnglishSymplectic Elements at Oxford2003Baymann, FBarlow, NAubert, CSchoepp-Cothenet, BLeroy, GArmstrong, FA periplasmic electron-transfer protein, cytochrome c(555)(m) from Aquifex aeolicus contains a 62-residue N-terminal extension by which it is anchored to the membrane--most probably via a thioester bond to its N-terminal cysteine. This linker can act as a "rope" to tether the protein close to its reaction partners. Mimicking this principle, a recombinant cytochrome c(555)(m), expressed in Escherichia coli, has been attached covalently to a gold electrode modified with 6-mercaptohexan-1-ol. The "tethered" cytochrome c(555)(m) displays remarkably fast electron-transfer kinetics, with an electrochemical exchange rate constant k(0) of 1.4 x 10(4) s(-1). The results show that fast electron transfer is associated with weak interactions: importantly, the tethered cytochrome can explore many different orientations without escaping into solution. |
| spellingShingle | Baymann, F Barlow, N Aubert, C Schoepp-Cothenet, B Leroy, G Armstrong, F Voltammetry of a "protein on a rope". |
| title | Voltammetry of a "protein on a rope". |
| title_full | Voltammetry of a "protein on a rope". |
| title_fullStr | Voltammetry of a "protein on a rope". |
| title_full_unstemmed | Voltammetry of a "protein on a rope". |
| title_short | Voltammetry of a "protein on a rope". |
| title_sort | voltammetry of a protein on a rope |
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