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:
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.
Structural Basis for the Thermostability of Sulfur Oxygenase Reductases
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 SOR
AA
(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.
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