CATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONS
Electron self-exchange in solutions of the 'blue' copper protein plastocyanin is catalysed by the redox-inert multivalent cations Mg2+ or Co(NH3)3+6. Measurements of specific 1H-NMR line broadening with 50% reduced solutions in the presence of these cations show that electron exchange proc...
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| Format: | Journal article |
| Language: | English |
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1985
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| _version_ | 1797090688631832576 |
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| author | Armstrong, F Driscoll, P Hill, H |
| author_facet | Armstrong, F Driscoll, P Hill, H |
| author_sort | Armstrong, F |
| collection | OXFORD |
| description | Electron self-exchange in solutions of the 'blue' copper protein plastocyanin is catalysed by the redox-inert multivalent cations Mg2+ or Co(NH3)3+6. Measurements of specific 1H-NMR line broadening with 50% reduced solutions in the presence of these cations show that electron exchange proceeds through encounters of cation-protein complexes which dissociate at high ionic strength. In the presence of 8mM (5 equivalents/total protein) Co(NH3)3+6, with 10 mM cacodylate (pH*6.0) as background electrolyte, the bimolecular rate constant at 25°C is 7 × 104 M-1·s-1. For comparison, the 'electrostatically screened' rate constant measured in 0.1 M KCl in the absence of added multivalent cations is ~ 4 × 103 M1·s-1. Plastocyanin Electron self-exchange NMR Protein-protein interaction Multivalent cation Blue copper protein. © 1985. |
| first_indexed | 2024-03-07T03:22:16Z |
| format | Journal article |
| id | oxford-uuid:b7d480ef-3a86-4d26-a230-1732f8adaf02 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:22:16Z |
| publishDate | 1985 |
| record_format | dspace |
| spelling | oxford-uuid:b7d480ef-3a86-4d26-a230-1732f8adaf022022-03-27T04:51:26ZCATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONSJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b7d480ef-3a86-4d26-a230-1732f8adaf02EnglishSymplectic Elements at Oxford1985Armstrong, FDriscoll, PHill, HElectron self-exchange in solutions of the 'blue' copper protein plastocyanin is catalysed by the redox-inert multivalent cations Mg2+ or Co(NH3)3+6. Measurements of specific 1H-NMR line broadening with 50% reduced solutions in the presence of these cations show that electron exchange proceeds through encounters of cation-protein complexes which dissociate at high ionic strength. In the presence of 8mM (5 equivalents/total protein) Co(NH3)3+6, with 10 mM cacodylate (pH*6.0) as background electrolyte, the bimolecular rate constant at 25°C is 7 × 104 M-1·s-1. For comparison, the 'electrostatically screened' rate constant measured in 0.1 M KCl in the absence of added multivalent cations is ~ 4 × 103 M1·s-1. Plastocyanin Electron self-exchange NMR Protein-protein interaction Multivalent cation Blue copper protein. © 1985. |
| spellingShingle | Armstrong, F Driscoll, P Hill, H CATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONS |
| title | CATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONS |
| title_full | CATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONS |
| title_fullStr | CATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONS |
| title_full_unstemmed | CATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONS |
| title_short | CATALYSIS OF PLASTOCYANIN ELECTRON SELF-EXCHANGE BY REDOX-INERT MULTIVALENT CATIONS |
| title_sort | catalysis of plastocyanin electron self exchange by redox inert multivalent cations |
| work_keys_str_mv | AT armstrongf catalysisofplastocyaninelectronselfexchangebyredoxinertmultivalentcations AT driscollp catalysisofplastocyaninelectronselfexchangebyredoxinertmultivalentcations AT hillh catalysisofplastocyaninelectronselfexchangebyredoxinertmultivalentcations |