Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

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Title: Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison
Authors: Hernández, Karel | Berenguer-Murcia, Ángel | Rodrigues, Rafael C. | Fernández Lafuente, Roberto
Research Group/s: Materiales Carbonosos y Medio Ambiente
Center, Department or Service: Universidad de Alicante. Departamento de Química Inorgánica | Universidad de Alicante. Instituto Universitario de Materiales
Keywords: Enzyme inactivation by oxidation | Catalase | Chemical modification | Genetic modification | Immobilization | Lipase | Oxidase | Partition effect
Knowledge Area: Química Inorgánica
Issue Date: Nov-2012
Publisher: Bentham Science Publishers
Citation: Current Organic Chemistry. 2012, 16(22): 2652-2672. doi:10.2174/138527212804004526
Abstract: Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide “in situ” to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation. This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this “dangerous liaison”.
Sponsor: This work has been supported by grant CTQ2009-07568 from Spanish Ministerio de Ciencia e Innovación. A. Berenguer-Murcia thanks the Spanish Ministerio de Ciencia e Innovación for a Ramon y Cajal fellowship (RyC-2009-03813). Mr. Hernandez is a holder of a MAEC-AECID fellowship.
URI: http://hdl.handle.net/10045/40212
ISSN: 1385-2728 (Print) | 1875-5348 (Online)
DOI: 10.2174/138527212804004526
Language: eng
Type: info:eu-repo/semantics/article
Rights: © 2012 Bentham Science Publishers
Peer Review: si
Publisher version: http://dx.doi.org/10.2174/138527212804004526
Appears in Collections:INV - MCMA - Artículos de Revistas

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