Abstract
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.
Original language | English (US) |
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Pages (from-to) | 667-671 |
Number of pages | 5 |
Journal | Journal of Biological Inorganic Chemistry |
Volume | 2 |
Issue number | 5 |
DOIs | |
State | Published - Oct 1997 |
Externally published | Yes |
Keywords
- Manganese
- Oxygen radicals
- Spectroscopy
- Thermophiles
ASJC Scopus subject areas
- Biochemistry
- Inorganic Chemistry