Improving enzyme-electrode contacts by redox modification of cofactors

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 biocatalysts 1–3 . But most redox enzymes lack pathways that can transport an electron from their...

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Bibliographic Details
Published in:Nature (London) 1995-08, Vol.376 (6542), p.672-675
Main Authors: Riklin, Azalla, Katz, Eugenii, Wiliner, Itamar, Stocker, Achim, Bückmann, Andreas F
Format: Article
Language:English
Subjects:
Apoproteins - chemistry
Biological and medical sciences
Biosensors
Biotechnology
Catalysis
D-Amino-Acid Oxidase - chemistry
Electrochemistry
Electrodes
Electrons
Enzymes
Ethyldimethylaminopropyl Carbodiimide - chemistry
Ferrous Compounds - chemistry
Flavin-Adenine Dinucleotide - chemistry
Fundamental and applied biological sciences. Psychology
Glucose Oxidase - chemistry
Humanities and Social Sciences
letter
Methods. Procedures. Technologies
multidisciplinary
Oxidation-Reduction
Polymers
Proteins
Science
Science (multidisciplinary)
Various methods and equipments
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Summary: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 biocatalysts 1–3 . But most redox enzymes lack pathways that can transport an electron from their embedded redox site to an electrode 4,5 or a diffusing photoexcited species 6 . Electrical communication between redox proteins and electrode surfaces has been improved by aligning proteins on chemically modified electrodes 7–9 , by attaching electron-transporting groups 10,11 and by immobilizing proteins in polymer matrices tethered by redox groups 12–14 . 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/376672a0