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

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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.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, P. O. Box 91000, Portland, OR 97291-1000, USA Tel.: +1-503-690-1065; Fax: 503-690-1464; e-mail: jim@insight.cbs.ogi.edu, , , , , , US

    M. M. Whittaker & J. W. Whittaker

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  1. M. M. Whittaker
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  2. J. W. Whittaker
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Received: 2 May 1997 / Accepted: 17 July 1997

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Whittaker, M., Whittaker, J. A "thermophilic shift" in ligand interactions for Thermus thermophilus manganese superoxide dismutase. JBIC 2, 667–671 (1997). https://doi.org/10.1007/s007750050182

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  • DOI: https://doi.org/10.1007/s007750050182

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