Structural basis for endoperoxide-forming oxygenases. Structure-based engineering of α-ketoglutarate dependent oxygenases in fungal meroterpenoid biosynthesis.
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Suppression of rebound may thus be generally important for nonhydroxylation outcomes by these enzymes. In all three cases, substrate hydroxylation incorporates a greater fraction of solvent-derived oxygen at the site that can also undergo the alternative outcome than at the other site, most likely reflecting an increased exchange of the initially O 2-derived oxygen ligand in the longer-lived Fe(III)-OH/R We evaluated this prediction for (i) the halogenase SyrB2, which exclusively hydroxylates C5 of norvaline appended to its carrier protein but can either chlorinate or hydroxylate C4 and (ii) two bifunctional enzymes that normally hydroxylate one carbon before coupling that oxygen to a second carbon (producing an oxacycle) but can, upon encountering deuterium at the first site, hydroxylate the second site instead. Here, we explored the general implication that, when a ferryl intermediate can ambiguously target two substrate carbons for different outcomes, rebound to the site capable of the alternative outcome should be slower than to the adjacent, solely hydroxylated site. We previously suggested that halogenases control substrate-cofactor disposition to disfavor oxygen rebound and permit halogen coupling to prevail. coupling to a halogen ligand cis to the hydroxide.state for example, halogenation results from R.Nonhydroxylation outcomes result from different fates of the Fe(III)-OH/R ) and oxygen of the Fe(III)-OH complex (“oxygen rebound”).
Hydroxylation proceeds by coupling of the resultant substrate radical (R Iron(II)- and 2-oxoglutarate-dependent (Fe/2OG) oxygenases generate iron(IV)-oxo (ferryl) intermediates that can abstract hydrogen from aliphatic carbons (R–H).
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