Structural Basis for the Thermostability of Sulfur Oxygenase Reductases

尤晓颜; 孟珍; 陈栋炜; 郭旭; Josef Zeyer; 刘双江; 姜成英

doi:10.1016/S1004-9541(12)60363-2

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Structural Basis for the Thermostability of Sulfur Oxygenase Reductases

Updated：2026-01-06

- Structural Basis for the Thermostability of Sulfur Oxygenase Reductases
- Structural Basis for the Thermostability of Sulfur Oxygenase Reductases
- 中国化学工程学报（英文版） 2012年20卷第1期页码：52-61
- Affiliations：
  
  1. State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences,Beijing,China,100101
  2. Scientific Data Center, Computer Network Information Center, Chinese Academy of Sciences,Beijing,China,100190
  3. Environmental Microbiology, Institute for Biogeochemistry and Pollutant Dynamics(IBP), Federal Institute of Technology(), Switzerland,ETH
- Author bio：
- Funds：
  
  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)
- DOI：10.1016/S1004-9541(12)60363-2
  中图分类号： Q55
- 纸质出版：2012
- Accepted：
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尤晓颜, 孟珍, 陈栋炜, 等. Structural Basis for the Thermostability of Sulfur Oxygenase Reductases[J]. 中国化学工程学报（英文版）, 2012,20(1):52-61.

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, 等. Structural Basis for the Thermostability of Sulfur Oxygenase Reductases[J]. 中国化学工程学报（英文版）, 2012,20(1):52-61. DOI： 10.1016/S1004-9541(12)60363-2.

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. DOI： 10.1016/S1004-9541(12)60363-2.

摘要

中图分类号:

Abstract

The thermostability of three sulfur oxygenase reductases(SORs) was investigated from thermoacidophilic achaea

Acidianus tengchongensis

(SOR

) and

Sulfolobus tokodaii

(SOR

) as well as the moderately thermophilic bacterium

Acidithiobacillus

sp.SM-1(SOR

).The optimal temperatures for catalyzing sulfur oxidation were 80℃(SORAT)

85℃(SORST)

and 70(SOR

)

respectively.The half-lives of the three SORs at their optimal catalytic conditions were 100 min(SORAT)

58 min(SOR

)

and 37 min(SOR

).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 SOR

(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

(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.

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