1.14.99.67	physiological function	CmlI is a non-heme di-iron enzyme catalyzing N-oxygenation of an amine group, one of the steps in the biosynthesis of the antibiotic chloramphenicol	
1.14.99.67	physiological function	diferrous CmlI can react with NH2-chloramphenicol species and O2 in either order to form a peroxo-NH2-chloramphenicol intermediate. Peroxo-NH2-chloramphenicol undergoes rapid oxygen transfer to form a diferric CmlI complex with the aryl-hydroxylamine [NH(OH)-chloramphenicol] pathway intermediate. Diferric CmlI-NH(OH)-chloramphenicol undergoes a rapid internal redox reaction to form a differous CmlI-nitroso-chloramphenicol complex. O2 binding results in formation of peroxo-NO-chloramphenicol that converts to differic CmlI-chloramphenicol by enzyme-mediated oxygen atom transfer. There is little dissociation of pathway intermediates as the reaction progresses	
1.14.99.67	physiological function	during the catalytic cycle substrate N-[(1R,2R)-1-(4-aminophenyl)-1,3-dihydroxypropan-2-yl]-2,2-dichloroacetamide reacts with a long-lived peroxo intermediate to form a NH(OH)-chloramphenicol species and diferric CmlI. Then the NH(OH)-chloramphenicol re-reduces the enzyme diiron cluster, allowing the peroxo species to re-form upon O2 binding, while itself being oxidized to NO-chloramphenicol. Finally, the re-formed peroxo species oxidizes NO-chloramphenicol to chloramphenicol with incorporation of a second O2-derived oxygen atom. The complete six-electron oxidation requires only two exogenous electrons and may occur in one active site	
1.14.99.67	physiological function	the key oxygenated intermediates in diiron arylamine oxygenases AurF, EC 1.14.99.68, and CmlI, so-called P, are uniformly hydroperoxo species having similar structures rather than the believed peroxo species. A diferric-hydroperoxo P is proposed to be able to promote the arylamine N-oxygenation with highly accessible kinetics