A surface-immobilized cytochrome c variant provides a pH-controlled molecular switch
| Autor: | Antonio Ranieri, Marco Borsari, Stefano Monari, Licia Paltrinieri, Marco Sola, Gianantonio Battistuzzi, Carlo Augusto Bortolotti |
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| Rok vydání: | 2012 |
| Předmět: |
Molecular switch
chemistry.chemical_classification biology Chemistry Cytochrome c Substrate (chemistry) protein engineering General Chemistry Photochemistry Electrochemistry Redox Yeast molecular switch Crystallography cytochrome c Enzyme electrochemistry electrocatalysis biology.protein Conformational isomerism |
| Zdroj: | Chem. Sci.. 3:807-810 |
| ISSN: | 2041-6539 2041-6520 |
| DOI: | 10.1039/c1sc00821h |
| Popis: | The K72A/K73H/K79A mutant of yeast iso-1-cytochrome c immobilized on a conductive substrate reversibly interconverts between the native-like, His-Met heme-ligated form and a His-His-ligated conformer with remarkably different redox and enzymatic properties. This transition is activated by changing the pH in a narrow range around neutrality. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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