Coupling to Lysine-13 Promotes Electron Tunneling through Carboxylate-Terminated Alkanethiol Self-Assembled Monolayers to Cytochrome c
| Autor: | W. Reef Hardy, Kyoko Fujita, James R. Sprinkle, H. Li, Emanuel Margoliash, Harry B. Gray, Hiroyuki Ohno, John H. Richards, Nobufumi Nakamura, Katsumi Niki, Michael G. Hill, Ryutaro Tanimura |
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| Rok vydání: | 2003 |
| Předmět: |
Alanine
biology Stereochemistry Cytochrome c Lysine Self-assembled monolayer Electrochemistry complex mixtures Surfaces Coatings and Films chemistry.chemical_compound Electron transfer Crystallography chemistry Monolayer Materials Chemistry biology.protein bacteria Carboxylate Physical and Theoretical Chemistry |
| Zdroj: | The Journal of Physical Chemistry B. 107:9947-9949 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/jp035392l |
| Popis: | Electrochemistry of surface-modified cytochrome c (cyt c) bound electrostatically to carboxylate-terminated alkanethiol self-assembled monolayers (SAM) reveals highly anisotropic electronic coupling across the protein/monolayer interface. Substitution of a lysine residue with alanine at position 13 in recombinant rat cyt c (RC9-K13A) lowers the interfacial electron transfer (ET) rate more than 5 orders of magnitude, whereas ET is only slightly affected by replacement of lysine-72 or lysine-79 with alanine. The results clearly show that lysine-13 is directly involved in coupling the protein to the SAM carboxylate terminus. Interfacial ET rates for both yeast iso-1 cyt c and the mutant RC9-K13R indicate that arginine-13 couples the protein to the carboxylate interface less well than lysine-13. |
| Databáze: | OpenAIRE |
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