The tunnelling conductance of molecularly ordered metalloprotein arrays.
Metalloproteins can be self-assembled in molecularly ordered, electrochemically addressable arrays. We report here on a study of the transport characteristics of the blue copper protein, azurin, from Pseudomonas aeruginosa, by a combination of electrochemical and scanning probe techniques (scanning...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2004
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| _version_ | 1826293618607915008 |
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| author | Davis, J Wrathmell, C Zhao, J Fletcher, J |
| author_facet | Davis, J Wrathmell, C Zhao, J Fletcher, J |
| author_sort | Davis, J |
| collection | OXFORD |
| description | Metalloproteins can be self-assembled in molecularly ordered, electrochemically addressable arrays. We report here on a study of the transport characteristics of the blue copper protein, azurin, from Pseudomonas aeruginosa, by a combination of electrochemical and scanning probe techniques (scanning tunnelling microscopy and conducting atomic force microscopy). Redox-switchable chemisorbed molecular arrays can be formed from both wild-type and mutant proteins using the strong affinity of cysteine residue thiolates for pristine gold surfaces. The molecular transconductance of single protein molecules within these arrays has been studied under controllable conditions where it has been additionally possible to resolve the effects of protein mechanical perturbation. Although tunnelling appears to be non-resonant and adequately explained through the use of a square barrier model, under some conditions the contribution of the redox-active copper centre to conductance is resolvable. |
| first_indexed | 2024-03-07T03:32:55Z |
| format | Journal article |
| id | oxford-uuid:bb51562b-a8e3-4131-87fa-18821005608e |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:32:55Z |
| publishDate | 2004 |
| record_format | dspace |
| spelling | oxford-uuid:bb51562b-a8e3-4131-87fa-18821005608e2022-03-27T05:16:07ZThe tunnelling conductance of molecularly ordered metalloprotein arrays.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bb51562b-a8e3-4131-87fa-18821005608eEnglishSymplectic Elements at Oxford2004Davis, JWrathmell, CZhao, JFletcher, JMetalloproteins can be self-assembled in molecularly ordered, electrochemically addressable arrays. We report here on a study of the transport characteristics of the blue copper protein, azurin, from Pseudomonas aeruginosa, by a combination of electrochemical and scanning probe techniques (scanning tunnelling microscopy and conducting atomic force microscopy). Redox-switchable chemisorbed molecular arrays can be formed from both wild-type and mutant proteins using the strong affinity of cysteine residue thiolates for pristine gold surfaces. The molecular transconductance of single protein molecules within these arrays has been studied under controllable conditions where it has been additionally possible to resolve the effects of protein mechanical perturbation. Although tunnelling appears to be non-resonant and adequately explained through the use of a square barrier model, under some conditions the contribution of the redox-active copper centre to conductance is resolvable. |
| spellingShingle | Davis, J Wrathmell, C Zhao, J Fletcher, J The tunnelling conductance of molecularly ordered metalloprotein arrays. |
| title | The tunnelling conductance of molecularly ordered metalloprotein arrays. |
| title_full | The tunnelling conductance of molecularly ordered metalloprotein arrays. |
| title_fullStr | The tunnelling conductance of molecularly ordered metalloprotein arrays. |
| title_full_unstemmed | The tunnelling conductance of molecularly ordered metalloprotein arrays. |
| title_short | The tunnelling conductance of molecularly ordered metalloprotein arrays. |
| title_sort | tunnelling conductance of molecularly ordered metalloprotein arrays |
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