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

Mei M. Whittaker; James W. Whittaker

doi:10.1007/s007750050182

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

Mei M. Whittaker, James W. Whittaker

Center for Coastal Margins

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	667-671
Number of pages	5
Journal	Journal of Biological Inorganic Chemistry
Volume	2
Issue number	5
DOIs	https://doi.org/10.1007/s007750050182
State	Published - Oct 1997

Keywords

Manganese
Oxygen radicals
Spectroscopy
Thermophiles

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

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10.1007/s007750050182

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title = "A 'thermophilic shift' in ligand interactions for Thermus thermophilus manganese superoxide dismutase",

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.",

keywords = "Manganese, Oxygen radicals, Spectroscopy, Thermophiles",

author = "Whittaker, {Mei M.} and Whittaker, {James W.}",

note = "Funding Information: Acknowledgements Support for this project from the National Institutes of Health (GM 42680) is gratefully acknowledged.",

year = "1997",

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T1 - A 'thermophilic shift' in ligand interactions for Thermus thermophilus manganese superoxide dismutase

AU - Whittaker, Mei M.

AU - Whittaker, James W.

N1 - Funding Information: Acknowledgements Support for this project from the National Institutes of Health (GM 42680) is gratefully acknowledged.

PY - 1997/10

Y1 - 1997/10

N2 - 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.

AB - 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.

KW - Manganese

KW - Oxygen radicals

KW - Spectroscopy

KW - Thermophiles

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