This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. The enzyme is a dimeric heme-protein oxidase that catalyses the oxidative dimerization of two L-tryptophan-derived molecules to form dichlorochromopyrrolic acid, the precursor for the fused six-ring indolocarbazole scaffold of rebeccamycin . Contains one molecule of heme b per monomer, as well as non-heme iron that is not part of an iron-sulfur center . In vivo the enzyme uses hydrogen peroxide, formed by the enzyme upstream in the biosynthetic pathway (EC 18.104.22.168, 7-chloro-L-tryptophan oxidase) as the electron acceptor. However, the enzyme is also able to catalyse the reaction using molecular oxygen .
EC 22.214.171.124 created 2010 as EC 126.96.36.199, transferred 2013 to EC 188.8.131.52, transferred 2016 to EC 184.108.40.206