2009
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Abstract: Cytochrome P450 monooxygenase and superoxide reductase (SOR) have the same first atom coordination shell at their iron active sites: an Fe[N(4)S] center in a square-pyramidal geometry with the sixth coordinate site open for the catalytic reaction. Furthermore, both pass through ferric hydroperoxo intermediates. Despite these similarities, the next step in their catalytic cycle is very different: distal oxygen protonation and O-O cleavage (P450) versus proximal oxygen protonation and H(2)O(2) release (SOR). One… Show more

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“…[12][13][14][15][16] In this catalytic process, each oxidation step consumes one mol of NADPH, one mol of molecular oxygen and requires of the presence of the cytochrome P450 reductase (CPR) as a source of electrons. 10,[17][18][19][20][21][22] The overall process of aromatization of androgens via the enzyme aromatase has been depicted in Scheme 1.…”
Section: Introductionmentioning
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“…[12][13][14][15][16] In this catalytic process, each oxidation step consumes one mol of NADPH, one mol of molecular oxygen and requires of the presence of the cytochrome P450 reductase (CPR) as a source of electrons. 10,[17][18][19][20][21][22] The overall process of aromatization of androgens via the enzyme aromatase has been depicted in Scheme 1.…”
Section: Introductionmentioning
“…Specifically, aromatase is involved in the formation of C 18 -estrogens, estrone (E1), 17β-estradiol (E2), and 17β,16α-estriol (E3), from the C 19 -androgens, androstenedione (ASD), testosterone (TST), and 16α-hydroxytestosterone (HTST), respectively. , In fact, this is the only known enzyme involved in the biosynthesis of estrogens from androgens in vertebrates . This conversion consists of the aromatization of the A ring of the androgens, which occurs through a process of three consecutive oxidations of the angular C 19 -methyl group of the androgens. In this catalytic process, each oxidation step consumes 1 mol of NADPH, 1 mol of molecular oxygen, and requires the presence of the cytochrome P450 reductase (CPR) as a source of electrons. , The overall process of aromatization of androgens via the enzyme aromatase has been depicted in Scheme .…”
Section: Introductionmentioning
“…Although some experimental studies have been reported on the catalytic activity of nonheme iron(III)–hydroperoxo complexes, there are very few computational studies in the field and none of the computational studies explains the differences between heme and nonheme iron(III)–hydroperoxo. [ 26 , 27 ] In order to gain insight into the ability of nonheme iron(III)–hydroperoxo intermediates in aromatic hydroxylation processes and the relative activity versus an iron(IV)–oxo species, we decided to do a density functional theory (DFT) study on the catalytic activity of [(L 5 2 )Fe III (OOH)] 2+ with aromatic substrates and perform a general analysis of nonheme versus heme iron(III)–hydroperoxo complexes and their potential reactivity in oxygen atom transfer. Our calculations show, for the first time, that nonheme iron(III)–hydroperoxo complexes can react with substrates efficiently through OH transfer to aromatic rings.…”
Section: Introductionmentioning
“…These results are interesting in light of the proposals for the mechanism of SOR, which must release H 2 O 2 via Fe-O bond cleavage and avoid O-O cleavage. Some evidence suggests that an Fe III -OO(H) intermediate in SOR should be high-spin, including recent DFT calculations,55 and the high-spin state may help to favor release of H 2 O 2 . 28 However, definitive evidence regarding the structure and spin-state of peroxo intermediate(s) in the native reaction of SOR with superoxide remains to be obtained.…”
Section: Discussionmentioning