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- W2079657825 abstract "Molecular oxygen is an abundant and inexpensive reagent which can effect a variety of useful oxidation reactions; dioxygen is thus an attractive oxidizing agent and is also highly desirable when environmental requirements are considered. However, due to its biradical nature, dioxygen reacts with organic substrates preferably according to a radical chain mechanism, which generally operates with low selectivity. This radical reaction pathway may be eliminated by activation of the dioxygen through coordination to a metal centre; the coordination is generally followed by transfer of electrons from the metal to the oxygen moiety. In living systems, metalloporphyrin complexes embedded in a protein environment are often responsible for binding and transport of dioxygen, as well as for incorporation of one or two oxygen atoms to the organic substrate via mono-or dioxygenase systems. This former action is effected by a monooxygenase enzyme such as cytochrome P-450 which contains iron protoporphyrin IX as the prosthetic group with an axial thiolate ligand provided by a cysteinyl amino acid residue of the protein. Investigations on the structure and oxidizing ability of cytochrome P-450 as well as on the related biomimetic systems have been extensively developed [1–9]. These protein and model studies have brought about the scheme for P-450 activation of dioxygen by P-450 and related systems, which is depicted in Fig. 1." @default.
- W2079657825 created "2016-06-24" @default.
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- W2079657825 date "1994-01-01" @default.
- W2079657825 modified "2023-10-17" @default.
- W2079657825 title "Oxidations Catalyzed by Ruthenium Porphyrins" @default.
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- W2079657825 doi "https://doi.org/10.1007/978-94-017-2247-6_4" @default.
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