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Residue 345 of dibenzothiophene (DBT) sulfone monooxygenase is involved in C-S bond cleavage specificity of alkylated DBT sulfones.

作者信息

Konishi Jin, Maruhashi Kenji

机构信息

Bio-Refining Process Laboratory, Japan Cooperation Center, Petroleum, 1900 Sodeshi-cho, Shimizu, Shizuoka 424-0037, Japan.

出版信息

Biotechnol Lett. 2003 Jul;25(14):1199-202. doi: 10.1023/a:1024564430107.

DOI:10.1023/a:1024564430107
PMID:12967013
Abstract

Rhodococcus erythropolis IGTS8 that possesses dibenzothiophene sulfone monooxygenase mutated at residue 345 (Q345A), can degrade octyl sulfide on which the wild strain cannot grow. Residue 345 and the neighbouring residues were changed by site-directed mutagenesis. Only DszA changed at residue 345 gave an altered C-S bond cleavage pattern of 3-methyl DBT sulfone. This residue is therefore involved in C-S bond cleavage specifically for alkylated DBT sulfone.

摘要

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