Control and recognition of anionic ligands in myoglobin

Francesca Cutruzzolà, Carlo Travaglini Allocatelli, Paolo Ascenzi, Martino Bolognesi, Stephen G. Sligar, Maurizio Brunori

Research output: Contribution to journalArticle

Abstract

Equilibrium and kinetic experiments on site-directed mutants of a synthetic sperm whale myoglobin (Mb) gene have been performed. Results on the reactivity on both ferric and ferrous wild type and mutants Mb's are presented. Analysis of ligand binding to His(E7) Val and His(E7) Val-Thr(E10) Arg mutants compared to wild-type sperm whale, horse and Aplysia limaelna Mb's, shows that the introduction of an arginyl residue at the topological position E10 greatly enhances the stability of the various Mb:heme ligand adducts. Alternative mechanisms of ligand stabilization may therefore be operative in Mb's lacking the distal histidine.

Original languageEnglish
Pages (from-to)281-284
Number of pages4
JournalFEBS Letters
Volume282
Issue number2
DOIs
Publication statusPublished - May 6 1991

Keywords

  • Ligand binding
  • Myoglobin mutant
  • Protein engineering

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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  • Cite this

    Cutruzzolà, F., Allocatelli, C. T., Ascenzi, P., Bolognesi, M., Sligar, S. G., & Brunori, M. (1991). Control and recognition of anionic ligands in myoglobin. FEBS Letters, 282(2), 281-284. https://doi.org/10.1016/0014-5793(91)80495-O