Electrochemical Studies of CO2-Reducing Metalloenzymes |
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Authors: | Dr. Marta Meneghello Dr. Christophe Léger Dr. Vincent Fourmond |
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Affiliation: | CNRS, Aix-Marseille Université, Laboratoire de Bioénergétique et Ingénierie des Protéines, UMR 7281, Institut de Microbiologie de la Méditerranée, and, Institut Microbiologie, Bioénergies et Biotechnologie, 31 chemin J. Aiguier, 13402 Marseille Cedex 20, France |
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Abstract: | Only two enzymes are capable of directly reducing CO2: CO dehydrogenase, which produces CO at a [NiFe4S4] active site, and formate dehydrogenase, which produces formate at a mononuclear W or Mo active site. Both metalloenzymes are very rapid, energy-efficient and specific in terms of product. They have been connected to electrodes with two different objectives. A series of studies used protein film electrochemistry to learn about different aspects of the mechanism of these enzymes (reactivity with substrates, inhibitors…). Another series focused on taking advantage of the catalytic performance of these enzymes to build biotechnological devices, from CO2-reducing electrodes to full photochemical devices performing artificial photosynthesis. Here, we review all these works. |
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Keywords: | CO dehydrogenase formate dehydrogenase CO2 reduction protein film electrochemistry metalloenzymes |
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