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Improving enzyme–electrode contacts by redox modification of cofactors

Nature volume 376, pages 672–675 (1995)Cite this article

Abstract

EFFICIENT electron transfer of redox proteins to and from their environment is essential for the use of such proteins in biotechnological applications such as amperometric biosensors and photosynthetic biocatalysts1–3. But most redox enzymes lack pathways that can transport an electron from their embedded redox site to an electrode4,5 or a diffusing photoexcited species6. Electrical communication between redox proteins and electrode surfaces has been improved by aligning proteins on chemically modified electrodes7–9, by attaching electron-transporting groups10,11 and by immobilizing proteins in polymer matrices tethered by redox groups12–14. Generally these methods involve contacting the enzymes at random with electron relay units. Here we report an approach that allows site-specific positioning of electron-mediating units in redox proteins. We strip glucose oxidase of its flavin adenine dinucleotide (FAD) cofactors, modify the latter with redox-active ferrocene-containing groups, and then reconstitute the apoprotein with these modified cofactors. In this way, electrical contact between an electrode and the resulting enzyme in solution is greatly enhanced in a controlled and reproducible way.

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Authors and Affiliations

  1. Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, 91904, Israel

    Azalla Riklin, Eugenii Katz & Itamar Wiliner

  2. Gesellschaft für Biotechnologische Forschung, Department of Enzymology, Mascheroder Weg 1, D-38124, Braunschweig, Germany

    Achim Stocker & Andreas F. Bückmann

Authors
  1. Azalla Riklin
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  2. Eugenii Katz
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  3. Itamar Wiliner
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  4. Achim Stocker
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  5. Andreas F. Bückmann
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Riklin, A., Katz, E., Wiliner, I. et al. Improving enzyme–electrode contacts by redox modification of cofactors. Nature 376, 672–675 (1995). https://doi.org/10.1038/376672a0

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