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Your search keyword '"Liao, Yuanping"' showing total 12 results
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12 results on '"Liao, Yuanping"'

5. Prevalence and Related Factors of Insomnia Among Chinese Medical Staff in the Middle and Late Stage of COVID-19

Author

Liu, Dianying, primary, Liu, Shaohua, additional, Zhu, Lin, additional, Li, Dongbin, additional, Huang, Donghua, additional, Deng, Hongdong, additional, Guo, Huiyun, additional, Huang, Dan, additional, Liao, Yuanping, additional, Mao, Zhongzhen, additional, Miao, Qiumei, additional, Liu, Wanglin, additional, Xiu, Meihong, additional, and Zhang, Xiangyang, additional

Published
2020
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7. Structure of formaldehyde dehydrogenase fromPseudomonas aeruginosa: the binary complex with the cofactor NAD+

Author

Xinquan Wang, Wangluo Zhang, Yingming Wang, Jianfeng Ding, Xiaoyuan Ran, Lijun Cai, Dingli Wang, Zhu Huaxing, Liao Yuanping, Chen Shuai, and Shuang Wang

Subjects
Models, Molecular, Molecular Sequence Data, Biophysics, Formaldehyde, Crystallography, X-Ray, Biochemistry, Cofactor, chemistry.chemical_compound, Bacterial Proteins, Structural Biology, Oxidoreductase, Catalytic Domain, Escherichia coli, Genetics, Structural Communications, Formate, Amino Acid Sequence, Conserved Sequence, Formaldehyde dehydrogenase, chemistry.chemical_classification, biology, Pseudomonas putida, NAD, Condensed Matter Physics, biology.organism_classification, Aldehyde Oxidoreductases, Recombinant Proteins, Kinetics, Enzyme, chemistry, Structural Homology, Protein, Pseudomonas aeruginosa, biology.protein, NAD+ kinase, Protein Multimerization, Oxidation-Reduction, Protein Binding
Abstract

Formaldehyde dehydrogenase (FDH) is a member of the zinc-containing medium-chain alcohol dehydrogenase family which oxidizes toxic formaldehyde to formate using NAD(+) as an electron carrier. Three-dimensional structures have been reported for FDHs from several different species. Most FDHs are dependent on glutathione for catalysis, but the enzyme from Pseudomonas putida is an exception. In this structural communication, the recombinant production, crystallization and X-ray structure determination at 2.7 Å resolution of FDH from P. aeruginosa are described. Both the tetrameric assembly and the NAD(+)-binding mode of P. aeruginosa FDH are similar to those of P. putida FDH, which is in good agreement with the high sequence identity (87.97%) between these two proteins. Preliminary enzymatic kinetics studies of P. aeruginosa FDH also revealed a conserved glutathione-independent `ping-pong' mechanism of formaldehyde oxidization.

Published
2013

8. Expression, purification, and characterization of formaldehyde dehydrogenase from Pseudomonas aeruginosa

Author

Chen Shuai, Xiaoyuan Ran, Dingli Wang, Zhu Huaxing, Jianfeng Ding, Yingming Wang, Daru Lu, Wangluo Zhang, and Liao Yuanping

Subjects
chemistry.chemical_classification, biology, GroES, Molecular cloning, biology.organism_classification, GroEL, Molecular biology, Aldehyde Oxidoreductases, Pseudomonas putida, Cofactor, Recombinant Proteins, Enzyme, chemistry, Biochemistry, Bacterial Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein purification, Pseudomonas aeruginosa, biology.protein, Escherichia coli, Formaldehyde dehydrogenase, Biotechnology, Molecular Chaperones
Abstract

As a member of zinc-containing medium-chain alcohol dehydrogenase family, formaldehyde dehydrogenase (FDH) can oxidize toxic formaldehyde to less active formate with NAD(+) as a cofactor and exists in both prokaryotes and eukaryotes. Most FDHs are well known to be glutathione-dependent in the catalysis of formaldehyde oxidation, but the enzyme from Pseudomonas putida is an exception, which is independent of glutathione. To identify novel glutathione-independent FDHs from other bacterial strains and facilitate the corresponding structural and enzymatic studies, high-level soluble expression and efficient purification of these enzymes need to be achieved. Here, we present molecular cloning, expression, and purification of the FDH from Pseudomonas aeruginosa, which is a Gram-negative pathogenic bacterium causing opportunistic human infection. The FDH of P. aeruginosa shows high sequence identity (87.97%) with that of P. putida. Our results indicated that coexpression with molecular chaperones GroES, GroEL, and Tig has significantly attenuated inclusion body formation and improved the solubility of the recombinant FDH in Escherichiacoli cells. A purification protocol including three chromatographic steps was also established to isolate the recombinant FDH to homogeneity with a yield of ∼3.2 mg from 1L of cell culture. The recombinant P. aeruginosa FDH was properly folded and biologically functional, as demonstrated by the mass spectrometric, crystallographic, and enzymatic characterizations of the purified proteins.

Published
2013

11. A novel fluorescent probe for H 2 O 2 detection based on CdSe@ZnS quantum dots/Ag nanocluster hybrid.

Author

Zhou Z, Yang L, Huang L, Liao Y, Liu Y, and Xiao Q

Subjects
Animals, Cadmium Compounds chemistry, Metal Nanoparticles chemistry, Particle Size, Quantum Dots chemistry, Selenium Compounds chemistry, Silver chemistry, Spectrometry, Fluorescence, Sulfides chemistry, Surface Properties, Zinc Compounds chemistry, Fluorescent Dyes chemistry, Hydrogen Peroxide analysis, Milk chemistry
Abstract

The selective and quantitative detection of H 2 O 2 is important for its employment in physiological, environmental and industrial applications. In this paper, a sensitive and selective strategy for H 2 O 2 detection was established based on the fluorescence quenching of CdSe@ZnS quantum dots (QDs) by H 2 O 2 -mediated etching process of Ag nanoclusters (AgNCs). In this strategy, dihydrolipoic acid (DHLA) modified AgNCs were applied as H 2 O 2 response group, the existence of H 2 O 2 could initiate the oxidation of AgNCs and the production of Ag + . CdSe@ZnS QDs are very sensitive to Ag + , which could give rise to the effective fluorescence quenching of CdSe@ZnS QDs. Based on this strategy, the present fluorescent assay could realize the quantification detection of H 2 O 2 and the limit of detection is calculated to be 0.3 μM under the optimum conditions. Furthermore, CdSe@ZnS/AgNCs hybrid-based probe was applied to detecting H 2 O 2 in milk samples and showed a good recoveries results ranged from 95.8% to 112.0%, meaning the potential applicability of this strategy., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier B.V. All rights reserved.)

Published
2020
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12. Structure of formaldehyde dehydrogenase from Pseudomonas aeruginosa: the binary complex with the cofactor NAD+.

Author

Liao Y, Chen S, Wang D, Zhang W, Wang S, Ding J, Wang Y, Cai L, Ran X, Wang X, and Zhu H

Subjects
Aldehyde Oxidoreductases genetics, Aldehyde Oxidoreductases metabolism, Amino Acid Sequence, Bacterial Proteins genetics, Bacterial Proteins metabolism, Catalytic Domain, Conserved Sequence, Crystallography, X-Ray, Escherichia coli genetics, Formaldehyde metabolism, Kinetics, Models, Molecular, Molecular Sequence Data, NAD metabolism, Oxidation-Reduction, Protein Binding, Protein Multimerization, Pseudomonas aeruginosa enzymology, Pseudomonas aeruginosa genetics, Pseudomonas putida chemistry, Pseudomonas putida enzymology, Pseudomonas putida genetics, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Structural Homology, Protein, Aldehyde Oxidoreductases chemistry, Bacterial Proteins chemistry, Formaldehyde chemistry, NAD chemistry, Pseudomonas aeruginosa chemistry
Abstract

Formaldehyde dehydrogenase (FDH) is a member of the zinc-containing medium-chain alcohol dehydrogenase family which oxidizes toxic formaldehyde to formate using NAD(+) as an electron carrier. Three-dimensional structures have been reported for FDHs from several different species. Most FDHs are dependent on glutathione for catalysis, but the enzyme from Pseudomonas putida is an exception. In this structural communication, the recombinant production, crystallization and X-ray structure determination at 2.7 Å resolution of FDH from P. aeruginosa are described. Both the tetrameric assembly and the NAD(+)-binding mode of P. aeruginosa FDH are similar to those of P. putida FDH, which is in good agreement with the high sequence identity (87.97%) between these two proteins. Preliminary enzymatic kinetics studies of P. aeruginosa FDH also revealed a conserved glutathione-independent `ping-pong' mechanism of formaldehyde oxidization.

Published
2013
Full Text
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