Alkane hydroxylation catalyzed by metalloporhyrins : evidence for different active oxygen species with alkylhydroperoxides and iodosobenzene as oxidants.
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Reactivities of high valent manganese-oxo porphyrins in aqueous medium
2022, TetrahedronCitation Excerpt :The oxidants are necessary to synthesis Mn-oxo intermediates selectively in an aqueous medium. Such intermediate formation has been achieved by the reaction of Mn-porphyrins with oxygen atom sources such as PhIO [65,66], NaOCl [67,68], H2O2 [69,70], alkyl hydroperoxides [71], IO4− [72], or dioxygen associated with a reductant [73,74]. The reactivity studies reveal that each of these oxidant interacts differently, however, their capacity of producing Mn-oxo porphyrins as an active catalyst in undergoing epoxidation, C–H bond activation are nearly comparable.
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2021, Journal of Organometallic ChemistryInherent steroid 17α,20-lyase activity in defunct cytochrome P450 17A enzymes
2018, Journal of Biological ChemistryCitation Excerpt :We interpret the results in the context of formation of Compound I (FeO3+), which can proceed to yield all of the observed products (Fig. 10, B and C). There are important caveats in the use of alkyl hydroperoxides as oxygen surrogates (55), in that some of the reactions observed with these can be attributed to reactions involving alkoxy radicals (56). However, the generation of hydroxylated steroid products argues against the involvement of alkoxy radicals, which would be unlikely to use such chemistry.
Cytochrome P450 Enzymes
2018, Comprehensive Toxicology: Third EditionMechanism of 17α,20-lyase and new hydroxylation reactions of human cytochrome P450 17A1 <sup>18</sup>O labeling and oxygen surrogate evidence for a role of a perferryl oxygen
2016, Journal of Biological ChemistryCitation Excerpt :Many studies in the literature involve the use of alkyl hydroperoxides as oxygen surrogates for P450 reactions, beginning with Kadlubar et al. (54). However, although peracids can be used as reagents to generate P450 compound I (55), studies with alkyl hydroperoxides are problematic due to the production of radicals and their ensuing chemistry (46, 56). Some bacterial family 152 P450s appear to use H2O2 as a physiological cofactor (37, 57–59), and bacterial P450 101A1 (P450cam) was mutated to a species that could efficiently utilize H2O2 in reactions (60).
Catalyst design in oxidation chemistry; From KMnO<inf>4</inf> to artificial metalloenzymes
2014, Bioorganic and Medicinal ChemistryCitation Excerpt :This would serve to direct selectivity in favour of sterically less hindered sites, as well as minimise catalyst deactivation by the formation of oxo-bridged dimers. This approach was employed throughout the 1980s and early 1990s in several groups, including those of Groves,133 Nam,134 Khenkin,135 Suslick136 and Mansuy.137 One of the more promising examples of these so-called ‘bis pocket’ porphyrins was tetrakis(triphenylphenyl) porphyrin (TTPPP, Fig. 7), which gave some of the best regioselectivities known at the time for linear alkanes (21:48:16:15 for C-1:2:3:4 in the hydroxylation of n-octane).136