A ''thermophilic shift'' in ligand interactions for Thermus thermophilus manganese superoxide dismutase

被引：20
|
作者：
Whittaker, MM [1 ]
Whittaker, JW [1 ]
机构：
[1] OREGON GRAD INST SCI & TECHNOL,DEPT BIOCHEM & MOL BIOL,PORTLAND,OR 97291
来源：
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 1997年 / 2卷 / 05期
基金：
美国国家卫生研究院;
关键词：
spectroscopy; manganese; oxygen radicals; thermophiles;
D O I：
10.1007/s007750050182
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Manganese superoxide dismutase from the obligate thermophile Thermus thermophilus HB8 exhibits a thermal transition in azide complexes that resembles the behavior found for a mesophilic MnSD (from Escherichia coli) but shifted 85 degrees to higher temperature. The active-site structures of the two enzymes are virtually identical, yet the dynamical behavior is evidently distinct, apparently adapted to the physiological growth temperature for each organism. These results provide evidence for subtle tuning of structure for proteins that function in extreme physical environments.
引用
收藏
页码：667 / 671
页数：5
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