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Laccases (EC 1.10.3.2) are polyphenol oxidases that catalyse the oxidation of various aromatic compounds, particularly those with electron-donating groups such as phenols (−OH) and anilines (−NH2), by using molecular oxygen as an electron acceptor (Gianfreda et al. 1999).
SO was shown to oxidize sulfite by using molecular oxygen as an electron acceptor [ 16] by producing hydrogen peroxide.
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Multicopper oxidases and heme peroxidases involved in lignin degradation by oxidizing lignin subunits using molecular oxygen (electron acceptor) and extracellular hydrogen peroxide (co-substrate), respectively.
We demonstrate the first instance of alkene epoxidation at mild conditions using molecular oxygen by a manganese porphyrin containing MOF, MOF-525-Mn [Zr6O4(OH)4(MgC48H24O8N4Cl)3].
This is not necessarily the case for photo-oxidation of organic compounds using molecular oxygen.
Nanovanadia-supported nickel manganese oxide shows high activity and stability for the oxidation of benzyl alcohol using molecular oxygen as a source of oxygen.
Polyphenol oxidases (PPOs) are dicopper enzymes that oxidize ortho-diphenols to ortho-diquinones using molecular oxygen.
Although structurally not related, laccases and PPOs carry out similar phenolic oxidations using molecular oxygen [ 52].
It might be possible that these organisms use molecular oxygen formed by Cld.
This reaction uses molecular oxygen and is catalyzed by chlorophyllide a oxygenase (CAO).
Laccases are very attractive enzymes for application in green chemistry, because they use molecular oxygen and produce only water as a by-product.
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