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Carbon Dots as Versatile Photosensitizers for Solar-Driven Catalysis with Redox Enzymes

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Hutton, GAM 
Reuillard, Bertrand  ORCID logo
Martindale, BCM 
Caputo, CA 
Lockwood, CWJ 


Light-driven enzymatic catalysis is enabled by the productive coupling of a protein to a photosensitizer. Photosensitizers used in such hybrid systems are typically costly, toxic, and/or fragile, with limited chemical versatility. Carbon dots (CDs) are low-cost, nanosized light-harvesters that are attractive photosensitizers for biological systems as they are water-soluble, photostable, nontoxic, and their surface chemistry can be easily modified. We demonstrate here that CDs act as excellent light-absorbers in two semibiological photosynthetic systems utilizing either a fumarate reductase (FccA) for the solar-driven hydrogenation of fumarate to succinate or a hydrogenase (H2ase) for reduction of protons to H2. The tunable surface chemistry of the CDs was exploited to synthesize positively charged ammonium-terminated CDs (CD-NHMe2+), which were capable of transferring photoexcited electrons directly to the negatively charged enzymes with high efficiency and stability. Enzyme-based turnover numbers of 6000 mol succinate (mol FccA)−1 and 43,000 mol H2 (mol H2ase)−1 were reached after 24 h. Negatively charged carboxylate-terminated CDs (CD-CO2) displayed little or no activity, and the electrostatic interactions at the CD–enzyme interface were determined to be essential to the high photocatalytic activity observed with CD-NHMe2+. The modular surface chemistry of CDs together with their photostability and aqueous solubility make CDs versatile photosensitizers for redox enzymes with great scope for their utilization in photobiocatalysis.



Biocatalysis, Carbon, Clostridium acetobutylicum, Hydrogenase, Models, Molecular, Nanoparticles, Oxidation-Reduction, Photochemical Processes, Photosensitizing Agents, Protein Conformation, Shewanella, Succinate Dehydrogenase, Sunlight

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Journal of the American Chemical Society

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American Chemical Society
Biotechnology and Biological Sciences Research Council (BB/J000124/1)
Biotechnology and Biological Sciences Research Council (BB/K010220/1)
Engineering and Physical Sciences Research Council (EP/K039520/1)
European Commission (624997)
This work was supported by a Cambridge Australia Poynton PhD scholarship (to G.A.M.H.), the BBSRC (BB/K010220/1 to E.R. and BB/K009885/1 to J.N.B.), an Oppenheimer PhD scholarship (to B.C.M.M.), and a Marie Curie postdoctoral fellowship (GAN 624997 to C.A.C.).
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