Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O₂-dependent oxidation of primary alcohols.

ABSTRACT: Thiol dioxygenases are non-heme mononuclear iron enzymes that catalyze the O₂-dependent oxidation of free thiols (-SH) to produce the corresponding sulfinic acid (-SO₂^-). Previous chemical rescue studies identified a putative Fe^III-O₂^- intermediate that precedes substrate oxidation in Mus musculus cysteine dioxygenase (Mm CDO). Given that a similar reactive intermediate has been identified in the extradiol dioxygenase 2, 3-HCPD, it is conceivable that these enzymes share other mechanistic features with regard to substrate oxidation. To explore this possibility, enzymatic reactions with Mm CDO (as well as the bacterial 3-mercaptopropionic acid dioxygenase, Av MDO) were performed using a substrate analogue (2-mercaptoaniline,

SUBMITTER: Morrow WP 

PROVIDER: S-EPMC5616182 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature