Abstract
The activation of dioxygen in biological systems has been the focus of interest of biochemists, bioinorganic chemists, and physiologists for many years. A whole body of literature exists on this topic. Furthermore, special conferences have been devoted to this subject and one of the last of these meetings should be mentioned here whose proceedings have been published by King et al..1 Enzymes involved in direct oxygen activation are oxidases and oxygenases. Oxygenases introduce either one atom of dioxygen into substrate and reduce the other atom to water (monooxygenases) or transfer two oxygen atoms into substrate (dioxygenases). Oxidases can be divided in two-electron and four-electron transferring enzymes. The first group reduces dioxygen to hydrogen peroxide and the second one dioxygen to water. Most of the oxygenases as well as oxidases contain as prosthetic groups either flavin, iron (heme or non-heme) or copper.
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Messerschmidt, A. (1993). Ascorbate Oxidase Structure and Chemistry. In: Karlin, K.D., Tyeklár, Z. (eds) Bioinorganic Chemistry of Copper. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-6875-5_38
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DOI: https://doi.org/10.1007/978-94-011-6875-5_38
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