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13 results on '"Deng, Lin"'

7. Imbalanced Frequencies of Th17 and Treg Cells in Acute Coronary Syndromes Are Mediated by IL-6-STAT3 Signaling

Author

Ma, Yanhui, primary, Yuan, Xiangliang, additional, Deng, Lin, additional, Xu, Weiping, additional, Zheng, Yingxia, additional, Yue, Chaoyan, additional, Zhang, Guanghui, additional, Xie, Fang, additional, Yang, Yuan H., additional, Gantier, Michael P., additional, Liu, JunPing, additional, Xu, Dakang, additional, and Shen, Lisong, additional

Published
2013
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12. Sequence Heterogeneity in NS5A of Hepatitis C Virus Genotypes 2a and 2b and Clinical Outcome of Pegylated-Interferon/Ribavirin Therapy

Author

El-Shamy, Ahmed, primary, Shoji, Ikuo, additional, Kim, Soo-Ryang, additional, Ide, Yoshihiro, additional, Imoto, Susumu, additional, Deng, Lin, additional, Yoon, Seitetsu, additional, Fujisawa, Takashi, additional, Tani, Satoshi, additional, Yano, Yoshihiko, additional, Seo, Yasushi, additional, Azuma, Takeshi, additional, and Hotta, Hak, additional

Published
2012
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13. CotA, a Multicopper Oxidase from Bacillus pumilus WH4, Exhibits Manganese-Oxidase Activity.

Author

Su, Jianmei, Bao, Peng, Bai, Tenglong, Deng, Lin, Wu, Hui, Liu, Fan, and He, Jin

Subjects
MULTICOPPER oxidase, BACILLUS pumilus, MANGANESE, CHROMOGENIC compounds, BIOCHEMISTRY, MICROBIOLOGY, ENVIRONMENTAL chemistry, HEAVY metals
Abstract

Multicopper oxidases (MCOs) are a family of enzymes that use copper ions as cofactors to oxidize various substrates. Previous research has demonstrated that several MCOs such as MnxG, MofA and MoxA can act as putative Mn(II) oxidases. Meanwhile, the endospore coat protein CotA from Bacillus species has been confirmed as a typical MCO. To study the relationship between CotA and the Mn(II) oxidation, the cotA gene from a highly active Mn(II)-oxidizing strain Bacillus pumilus WH4 was cloned and overexpressed in Escherichia coli strain M15. The purified CotA contained approximately four copper atoms per molecule and showed spectroscopic properties typical of blue copper oxidases. Importantly, apart from the laccase activities, the CotA also displayed substantial Mn(II)-oxidase activities both in liquid culture system and native polyacrylamide gel electrophoresis. The optimum Mn(II) oxidase activity was obtained at 53°C in HEPES buffer (pH 8.0) supplemented with 0.8 mM CuCl2. Besides, the addition of o-phenanthroline and EDTA both led to a complete suppression of Mn(II)-oxidizing activity. The specific activity of purified CotA towards Mn(II) was 0.27 U/mg. The Km, Vmax and kcat values towards Mn(II) were 14.85±1.17 mM, 3.01×10−6±0.21 M·min−1 and 0.32±0.02 s−1, respectively. Moreover, the Mn(II)-oxidizing activity of the recombinant E. coli strain M15-pQE-cotA was significantly increased when cultured both in Mn-containing K liquid medium and on agar plates. After 7-day liquid cultivation, M15-pQE-cotA resulted in 18.2% removal of Mn(II) from the medium. Furthermore, the biogenic Mn oxides were clearly observed on the cell surfaces of M15-pQE-cotA by scanning electron microscopy. To our knowledge, this is the first report that provides the direct observation of Mn(II) oxidation with the heterologously expressed protein CotA, Therefore, this novel finding not only establishes the foundation for in-depth study of Mn(II) oxidation mechanisms, but also offers a potential biocatalyst for Mn(II) removal. [ABSTRACT FROM AUTHOR]

Published
2013
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