Abstract
A new concept for enzyme-catalyzed redox transformations features pairs of electron donor and acceptor enzymes attached to conducting particles. Electrons furnished by oxidation at one enzyme are used at the other. Graphite microparticles modified with hydrogenase and nitrate reductase or fumarate reductase catalyze reductions of nitrate or fumarate (1) by H2.
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Acknowledgements
This research was supported by grants from the UK Biotechnology and Biological Sciences Research Council (BB/D52222X/1), the UK Engineering and Physical Sciences Research Council (Supergen V) and the Leverhulme Trust (F/08699/C). J.H.W. is a Canada Research Chair and thanks the Alberta Heritage Foundation for Medical Research for a travel award. The authors thank N. Boroumand (University of Alberta), G. Cecchini (NCIRE Veterans Health Research Institute, San Francisco) and B. Friedrich (Humboldt-Universität zu Berlin), respectively, for samples of nitrate reductase, fumarate reductase and Ralstonia metallidurans hydrogenase (CH34).
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K.A.V. jointly designed the coupling experiments, jointly performed the nitrate reductase/hydrogenase experiments and jointly wrote the paper; X.L. jointly performed the nitrate reductase/hydrogenase experiments; C.F.B. jointly designed and conducted the fumarate reductase/hydrogenase experiments, carried out the SEM and N2 porosimetry and jointly wrote the paper; N.A.B. conducted the fumarate reductase/hydrogenase experiments and purified A. vinosum hydrogenase; J.H.W. jointly designed the coupling experiments and jointly wrote the paper; F.A.A. jointly designed the experiments and jointly wrote the paper.
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Supplementary Figures 1–3 and Supplementary Methods (PDF 323 kb)
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Vincent, K., Li, X., Blanford, C. et al. Enzymatic catalysis on conducting graphite particles. Nat Chem Biol 3, 761–762 (2007). https://doi.org/10.1038/nchembio.2007.47
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DOI: https://doi.org/10.1038/nchembio.2007.47
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