Ontology highlight
ABSTRACT:
SUBMITTER: Su T
PROVIDER: S-EPMC5819316 | biostudies-literature | 2018
REPOSITORIES: biostudies-literature
Su Tiantian T Su Jing J Liu Shiheng S Zhang Conggang C He Jing J Huang Yan Y Xu Sujuan S Gu Lichuan L
Frontiers in microbiology 20180215
Dibenzothiophene (DBT) and their derivatives, accounting for the major part of the sulfur components in crude oil, make one of the most significant pollution sources. The DBT sulfone monooxygenase BdsA, one of the key enzymes in the "4S" desulfurization pathway, catalyzes the oxidation of DBT sulfone to 2'-hydroxybiphenyl 2-sulfonic acid (HBPSi). Here, we determined the crystal structure of BdsA from <i>Bacillus subtilis</i> WU-S2B, at the resolution of 2.2 Å, and the structure of the BdsA-FMN c ...[more]