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

Mei M. Whittaker, James W. Whittaker

Research output: Contribution to journalArticle

15 Scopus citations

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 languageEnglish (US)
Pages (from-to)667-671
Number of pages5
JournalJournal of Biological Inorganic Chemistry
Volume2
Issue number5
DOIs
StatePublished - Oct 1 1997

Keywords

  • Manganese
  • Oxygen radicals
  • Spectroscopy
  • Thermophiles

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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