Both FMNH2 and FADH2 can be utilized by the dibenzothiophene monooxygenase from a desulfurizing bacterium Mycobacterium goodii X7B
Both FMNH2 and FADH2 can be utilized by the dibenzothiophene monooxygenase from a desulfurizing bacterium Mycobacterium goodii X7B
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FMNH2 和 FADH2 均可被脱硫细菌古氏分枝杆菌 X7B 的二苯并噻吩单加氧酶利用。
DOI：
10.1016/j.biortech.2008.12.009
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发表时间：
2009-05-01
影响因子：
11.4
通讯作者：
Xu, Ping
中科院分区：
文献类型：
--
作者：
Li, Jingchen;Feng, Jinhui;Xu, Ping
为研究二苯并噻吩单加氧酶（DszC）对黄素的利用，从重组大肠杆菌中分离纯化了一株古氏分枝杆菌X7 B的DszC。当与还原FMN或FAD的黄素还原酶偶联时，它能够利用FMNH 2或FADH（2）。序列分析表明，DszC与鲍曼不动杆菌对羟基苯乙酸羟化酶的C-2组分相似，能以FADH（2）和FMNH 2为底物。两种黄素在高浓度下均能抑制DszC的活性，这是由于还原型黄素的自催化氧化所致。结果表明，DszC应重新归类为FMNH 2和FADH（2）都利用单加氧酶组分，并应控制在适当降低的水平，以获得最佳的生物脱硫效果。(C)2008爱思唯尔有限公司保留所有权利。
To investigate the flavin utilization by dibenzothiophene monooxygenase (DszC), DszC of a desulfurizing bacterium Mycobacterium goodii X7B was purified from the recombinant Escherichia coli. It was shown to be able to utilize either FMNH2 or FADH(2) when coupled with a flavin reductase that reduces either FMN or FAD. Sequence analysis indicated that DszC was similar to the C-2 component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii, which can use both FADH(2) and FMNH2 as substrates. Both flavins at high concentrations could inhibit the activity of DszC due to autocatalytic oxidation of reduced flavins. The results suggest that DszC should be reclassified as an FMNH2 and FADH(2) both-utilizing monooxygenase component and the flavins should be controlled at properly reduced levels to obtain optimal biodesulfurization results. (C) 2008 Elsevier Ltd. All rights reserved.