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Sliding Helix and Change of Coordination Geometry in a Model Di-MnII Protein

Authors

  • William F. DeGrado Prof.,

    1. Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059A, USA
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  • Luigi Di Costanzo Dr.,

    1. Center of Excellence in Biocrystallography, Department of Chemical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy, Fax: (+39) 040-558-3903
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  • Silvano Geremia Prof.,

    1. Center of Excellence in Biocrystallography, Department of Chemical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy, Fax: (+39) 040-558-3903
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  • Angela Lombardi Prof.,

    1. Department of Chemistry, University of Naples “Federico II”, Complesso Universitario Monte S'Angelo, Via Cynthia 45, 80126 Naples, Italy
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  • Vincenzo Pavone Prof.,

    1. Department of Chemistry, University of Naples “Federico II”, Complesso Universitario Monte S'Angelo, Via Cynthia 45, 80126 Naples, Italy
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  • Lucio Randaccio Prof.

    1. Center of Excellence in Biocrystallography, Department of Chemical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy, Fax: (+39) 040-558-3903
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  • This work was supported by the MIUR (PRIN MM03185591), NIH grant GM54616, and by the MRSEC program of the NSF (award DMR0079909. We thank Ben North for many helpful discussions and preliminary calculations.

Abstract

original image

Ein synthetisches Metalloproteinbündel aus vier Helices hat zwei verschiedene Dimangan-Koordinationsumgebungen, die verbrückende oder terminale Solvensmoleküle enthalten. Ein Gleit-Helix-Mechanismus, durch den die Metalloproteine ihre Koordinationsumgebung ändern können, wird hier vorgestellt (siehe Bild).

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