Extrapolating the recent progress in the near future the extensive utilization of cofactor-dependent enzymes (enzymes of the 3rd generation) for solving economic or medical problems will be restricted by the difficulties of cofactor regeneration. Real possibilities exist in analytical systems, for instance enzyme electrodes. In the present paper a special case of overcoming the cofactor regeneration in P-450 catalyzed substrate hydroxylation is demonstrated: The peroxide-dependent reaction gives the same products as obtained under physiological conditions; that is why in an electro-enzyme-reactor producing hydrogen peroxide by cathodic oxygen reduction a considerable simplification of the multi-enzyme complex is possible by omitting electron transfer proteins. At present the main problem is the instability of the terminal oxidase. Attempts are being made to solve these problems by immobilizing the protein or substituting P-450 by other hemoproteins or iron porphyrin derivatives.
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Biol Methods Protoc
December 2024
Department of Biotechnology, Indian Institute of Technology Hyderabad (IITH), Sanga Reddy, Kandi, Telangana 502284, India.
Non-haem iron (Fe) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation of 2OG to the hydroxylation of the substrates. While some of these enzymes are reported to have multiple substrates, the substrate remains unknown for many of the enzymes.
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Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, SP, Brazil.
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Shandong Ocean Pipe Technology Co., Ltd, Dezhou 253300, China.
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College of Material and Chemical Engineering, Zhengzhou University of Light Industry, Zhengzhou, Henan 450002, China.
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College of Pharmacy, Dalian Medical University, Liaoning Dalian, China.
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