Thermostable Flavin Reductase That Couples with Dibenzothiophene Monooxygenase, from Thermophilic Bacillus sp. DSM411: Purification, Characterization, and Gene Cloning
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- OHSHIRO Takashi
- Department of Biotechnology, Tottori University
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- YAMADA Hiroko
- Department of Biotechnology, Tottori University
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- SHIMODA Tomohisa
- Department of Biotechnology, Tottori University
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- MATSUBARA Toshiyuki
- Department of Biotechnology, Tottori University
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- IZUMI Yoshikazu
- Department of Biotechnology, Tottori University
Bibliographic Information
- Other Title
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- Thermostable Flavin Reductase That Couples with Dibenzothiophene Monooxygenase, from Thermophilic<i>Bacillus</i>sp. DSM411: Purification, Characterization, and Gene Cloning
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Abstract
Flavin reductase is essential for the oxygenases involved in microbial dibenzothiophene (DBT) desulfurization. An enzyme of the thermophilic strain, Bacillus sp. DSM411, was selected to couple with DBT monooxygenase (DszC) from Rhodococcus erythropolis D-1. The flavin reductase was purified to homogeneity from Bacillus sp. DSM411, and the native enzyme was a monomer of Mr 16 kDa. Although the best substrates were flavin mononucleotide and NADH, the enzyme also used other flavin compounds and acted slightly on nitroaromatic compounds and NADPH. The purified enzyme coupled with DszC and had a ferric reductase activity. Among the flavin reductases so far characterized, the present enzyme is the most thermophilic and thermostable. The gene coded for a protein of 155 amino acids with a calculated mass of 17,325 Da. The enzyme was overproduced in Escherichia coli, and the specific activity in the crude extracts was about 440-fold higher than that of the wild-type strain, Bacillus sp. DSM411.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 68 (8), 1712-1721, 2004
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details
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- CRID
- 1390001206476301824
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- NII Article ID
- 10013520851
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 7066936
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- PubMed
- 15322355
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed