Accepted name: dibenzothiophene monooxygenase
Reaction: dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O (overall reaction)
(1a) dibenzothiophene + FMNH2 + O2 = dibenzothiophene-5-oxide + FMN + H2O
(1b) dibenzothiophene-5-oxide + FMNH2 + O2 = dibenzothiophene-5,5-dioxide + FMN + H2O
Glossary: dibenzothiophene-5,5-dioxide = dibenzothiophene sulfone
Other name(s): dszC (gene name)
Systematic name: dibenzothiophene,FMNH2:oxygen oxidoreductase
Comments: This bacterial enzyme catalyses the first two steps in the desulfurization pathway of dibenzothiophenes, the oxidation of dibenzothiophene into dibenzothiophene sulfone via dibenzothiophene-5-oxide. The enzyme forms a two-component system with a dedicated NADH-dependent FMN reductase (EC encoded by the dszD gene, which also interacts with EC, dibenzothiophene sulfone monooxygenase.
1.  Gray, K.A., Pogrebinsky, O.S., Mrachko, G.T., Xi, L., Monticello, D.J. and Squires, C.H. Molecular mechanisms of biocatalytic desulfurization of fossil fuels. Nat. Biotechnol. 14 (1996) 1705–1709. [PMID: 9634856]
2.  Liu, S., Zhang, C., Su, T., Wei, T., Zhu, D., Wang, K., Huang, Y., Dong, Y., Yin, K., Xu, S., Xu, P. and Gu, L. Crystal structure of DszC from Rhodococcus sp. XP at 1.79 Å. Proteins 82 (2014) 1708–1720. [PMID: 24470304]
3.  Guan, L.J., Lee, W.C., Wang, S., Ohshiro, T., Izumi, Y., Ohtsuka, J. and Tanokura, M. Crystal structures of apo-DszC and FMN-bound DszC from Rhodococcus erythropolis D-1. FEBS J. 282 (2015) 3126–3135. [PMID: 25627402]
[EC created 2016]