Regular ArticleChloroperoxidase-Catalyzed Benzylic Hydroxylation
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Advances in enzymatic oxyfunctionalization of aliphatic compounds
2021, Biotechnology AdvancesCitation Excerpt :Caldaromyces fumago). This enzyme typically performs halide oxidation and its peroxygenase activity is limited to epoxidation of styrene (Tuynman et al., 2000) and linear alkenes (Geigert et al., 1986), moderate hydroxylation of benzylic carbons (Miller et al., 1995) and sulfoxidations (Colonna et al., 1992; Manoj and Hager, 2001), while it is unable to perform oxygenation of stronger CH bonds. Aliphatic oxyfunctionalization reactions with UPOs have been described on a wide variety of substrates and, in most cases, with different regioselectivity depending on the enzyme used.
Optimizing the chloroperoxidase-glucose oxidase system: The effect of glucose oxidase on activity and enantioselectivity
2015, Process BiochemistryCitation Excerpt :In vivo it catalyzes the oxidative chlorination of 1,3-cyclopentadione by generating hypochlorite in situ by oxidation of chloride ion (reaction (3)). In the absence of halide ions it is able to catalyze a variety of synthetically useful oxygen insertions (see Fig. 1), such as: olefin epoxidation [10–13], sulfoxidation [14–16], hydroxylations [17–19], oxidation of indoles [20,21] and oxidation of primary alcohols to aldehydes [22–27]. This makes CPO a catalyst with an extremely high commercial potential.
Chloroperoxidase catalyzed oxidation of Cbz-ethanolamine to Cbz-glycinal
2012, Biochemical Engineering JournalCitation Excerpt :CPO catalyzed reactions can be divided in two main classes: reactions of halogenation catalyzed by acidic form of CPO (pH < 3) and non-halogenating reactions catalyzed by more neutral form of CPO (pH = 5–6) [1,3,4]. Within the class of non-halogenating reactions CPO was found to catalyze enantioselective sulfoxidation [5], epoxidation [6,7], benzylic hydroxylation [8], oxidation of amino into nitroso group [9] and oxidation of primary alcohols to aldehydes [10–12]. Catalase activity of CPO takes place in the absence of halide ion and organic substrate and results in the disproportionation of H2O2 to molecular oxygen and water [13].
Bienzymatic synthesis of benzothia/(oxa)zoles in aqueous medium
2010, Tetrahedron LettersStepwise oxygenations of toluene and 4-nitrotoluene by a fungal peroxygenase
2010, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Some other oxidative fungal enzymes such as lignin peroxidases and chloroperoxidases also have an extracellular location, but are more limited than AaeAPO in the variety of compounds they can utilize as electron donors. For example, lignin peroxidase does not oxidize benzyl alcohol, and neither of these peroxidases is able to oxidize 4-nitrotoluene [17,19,20]. The broad substrate range and ubiquitous distribution of extracellular APOs may indicate an important environmental role for them in the oxidation of both natural and anthropogenic aromatics.
Inactivation studies on native and silica gel non-homogeneous immobilized chloroperoxidase
2006, Journal of Molecular Catalysis B: Enzymatic