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Article

Crystal structures of TdsC, a dibenzothiophene monooxygenase from the thermophile Paenibacillus sp. A11-2, reveal potential for expanding its substrate selectivity.

The Journal of biological chemistry - 22 Sept 2017

Hino Tomoya, Hamamoto Haruka, Suzuki Hirokazu, Yagi Hisashi, Ohshiro Takashi, Nagano Shingo

Abstract excerpt

Sulfur compounds in fossil fuels are a major source of environmental pollution, and microbial desulfurization has emerged as a promising technology for removing sulfur under mild conditions. The enzyme TdsC from the thermophile Paenibacillus sp. A11-2 is a two-component flavin-dependent monooxygenase that catalyzes the oxygenation of dibenzothiophene (DBT) to its sulfoxide (DBTO) and sulfone (DBTO2) during...

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PMID: 28768765
DOI: 10.1074/jbc.M117.788513
PMCID: PMC5612111

Genes

DBT

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