Structural Basis for the Thermostability of Sulfur Oxygenase Reductases

›› 2012, Vol. 20 ›› Issue (1): 52-61.

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Structural Basis for the Thermostability of Sulfur Oxygenase Reductases

YOU Xiaoyan¹, MENG Zhen², CHEN Dongwei¹, GUO Xu¹, Josef Zeyer³, LIU Shuangjiang¹, JIANG Chengying¹

1. State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;
2. Scientific Data Center, Computer Network Information Center, Chinese Academy of Sciences, Beijing 100190, China;
3. Environmental Microbiology, Institute for Biogeochemistry and Pollutant Dynamics(IBP), Federal Institute of Technology(ETH), Switzerland

Received:2011-10-08 Revised:2011-12-19 Online:2012-05-03 Published:2012-02-28
Supported by:
Supported by the National Natural Science Foundation of China (31070042,30870039,30921065);partially by Open Funding Project of the National Key Laboratory of Biochemical Engineering,China (2010KF-2)

Structural Basis for the Thermostability of Sulfur Oxygenase Reductases

尤晓颜¹, 孟珍², 陈栋炜¹, 郭旭¹, Josef Zeyer³, 刘双江¹, 姜成英¹

1. State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;
2. Scientific Data Center, Computer Network Information Center, Chinese Academy of Sciences, Beijing 100190, China;
3. Environmental Microbiology, Institute for Biogeochemistry and Pollutant Dynamics(IBP), Federal Institute of Technology(ETH), Switzerland

通讯作者: LIU Shuangjiang,E-mail:liusj@sun.im.ac.cn;JIANG Chengying,E-mail:jiangcy@im.ac.cn
基金资助:
Supported by the National Natural Science Foundation of China (31070042,30870039,30921065);partially by Open Funding Project of the National Key Laboratory of Biochemical Engineering,China (2010KF-2)

Abstract

Abstract: The thermostability of three sulfur oxygenase reductases(SORs) was investigated from thermoacidophilic achaea Acidianus tengchongensis(SOR_AT) and Sulfolobus tokodaii(SOR_ST) as well as the moderately thermophilic bacterium Acidithiobacillus sp.SM-1(SOR_SB).The optimal temperatures for catalyzing sulfur oxidation were 80℃(SORAT),85℃(SORST),and 70(SOR_SB),respectively.The half-lives of the three SORs at their optimal catalytic conditions were 100 min(SORAT),58 min(SOR_ST),and 37 min(SOR_SB).In order to reveal the structural basis of the thermostability of these SORs,three-dimensional structural models of them were generated by homology modeling using the previously reported high-resolution X-ray structure of SORAA(from Acidianus ambivalens) as a template.The results suggest that thermostability was dependent on:(a) high number of the charged amino acid glutamic acid and the flexible amino acid proline,(b) low number of the thermolabile amino acid glutamine,(c) increased number of ion pairs,(d) decreased ratio of hydrophobic accessible solvent surface area(ASA) to charged ASA,and(e) increased volumes of the cavity.The number of cavities and the number of hydrogen bonds did not significantly affect the thermostability of SORs,whereas the cavity volumes increased as the thermal stability increased.

Key words: sulfur oxygenase reductase(SOR), thermostability, homology modeling, Acidianus,Sulfolobus,Acid-ithiobacillus

摘要： The thermostability of three sulfur oxygenase reductases(SORs) was investigated from thermoacidophilic achaea Acidianus tengchongensis(SOR_AT) and Sulfolobus tokodaii(SOR_ST) as well as the moderately thermophilic bacterium Acidithiobacillus sp.SM-1(SOR_SB).The optimal temperatures for catalyzing sulfur oxidation were 80℃(SORAT),85℃(SORST),and 70(SOR_SB),respectively.The half-lives of the three SORs at their optimal catalytic conditions were 100 min(SORAT),58 min(SOR_ST),and 37 min(SOR_SB).In order to reveal the structural basis of the thermostability of these SORs,three-dimensional structural models of them were generated by homology modeling using the previously reported high-resolution X-ray structure of SORAA(from Acidianus ambivalens) as a template.The results suggest that thermostability was dependent on:(a) high number of the charged amino acid glutamic acid and the flexible amino acid proline,(b) low number of the thermolabile amino acid glutamine,(c) increased number of ion pairs,(d) decreased ratio of hydrophobic accessible solvent surface area(ASA) to charged ASA,and(e) increased volumes of the cavity.The number of cavities and the number of hydrogen bonds did not significantly affect the thermostability of SORs,whereas the cavity volumes increased as the thermal stability increased.

关键词: sulfur oxygenase reductase(SOR), thermostability, homology modeling, Acidianus,Sulfolobus,Acid-ithiobacillus

CLC Number:

YOU Xiaoyan, MENG Zhen, CHEN Dongwei, GUO Xu, Josef Zeyer, LIU Shuangjiang, JIANG Chengying. Structural Basis for the Thermostability of Sulfur Oxygenase Reductases[J]. , 2012, 20(1): 52-61.

尤晓颜, 孟珍, 陈栋炜, 郭旭, Josef Zeyer, 刘双江, 姜成英. Structural Basis for the Thermostability of Sulfur Oxygenase Reductases[J]. , 2012, 20(1): 52-61.

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Structural Basis for the Thermostability of Sulfur Oxygenase Reductases

Structural Basis for the Thermostability of Sulfur Oxygenase Reductases

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