Control and recognition of anionic ligands in myoglobin

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

doi:10.1016/0014-5793(91)80495-O

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	281-284
Number of pages	4
Journal	FEBS Letters
Volume	282
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(91)80495-O
State	Published - May 6 1991

Keywords

Ligand binding
Myoglobin mutant
Protein engineering

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Online availability

10.1016/0014-5793(91)80495-O

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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.",

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T1 - Control and recognition of anionic ligands in myoglobin

AU - Cutruzzolà, Francesca

AU - Allocatelli, Carlo Travaglini

AU - Ascenzi, Paolo

AU - Bolognesi, Martino

AU - Sligar, Stephen G.

AU - Brunori, Maurizio

PY - 1991/5/6

Y1 - 1991/5/6

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AB - 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.

KW - Ligand binding

KW - Myoglobin mutant

KW - Protein engineering

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Control and recognition of anionic ligands in myoglobin

Abstract

Keywords

ASJC Scopus subject areas

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