Coupling to Lysine-13 Promotes Electron Tunneling through Carboxylate-Terminated Alkanethiol Self-Assembled Monolayers to Cytochrome c
Creators
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1.
California Institute of Technology
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2.
Tokyo University of Agriculture and Technology
Abstract
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.
Additional Information
© 2003 American Chemical Society. Received: May 20, 2003. The authors thank Dojindo Molecular Technology for providing carboxylic acid-terminated alkanethiols. Work at Occidental College was supported by the David and Lucille Packard Foundation's Initiative for Interdisciplinary Research. Work at Caltech was supported by NIH DK19038, NSF, and the Arnold and Mabel Beckman Foundation. E.M., H.L., and JS acknowledge support from the Edward Mallinckrodt, Jr. Foundation. K.F. thanks the Japan Society for the Promotion of Science (Research Fellowships for Young Scientists) for support.Additional details
Identifiers
- Eprint ID
- 57055
- Resolver ID
- CaltechAUTHORS:20150428-140736351
Funding
- David and Lucille Packard Foundation
- NIH
- DK19038
- NSF
- Arnold and Mabel Beckman Foundation
- Edward Mallinckrodt, Jr. Foundation
- Japan Society for the Promotion of Science (JSPS)
Dates
- Created
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2015-04-28Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field