Control and recognition of anionic ligands in myoglobin

FEBS Letters

Sligar, Stephen G.²  Ascenzi, Paolo¹  Cutruzzolà, Francesca¹  Brunori, Maurizio¹  Bolognesi, Martino³  Allocatelli, Carlo Travaglini¹ 

[1] Department of Biochemical Sciences and CNR Center for Molecular Biology, University of Rome ‘La Sapienza’, 00185 Rome, Italy;Department of Chemistry and Biochemistry, University of Illinois at Urbana, Roger Adams Laboratory, Urbana, IL 61801, USA;Department of Genetics and Microbiology, Section of Crystallography, University of Pavia, 27100 Pavia, Italy

关键词: Protein engineering;    Myoglobin mutant;    Ligand binding;    Mb;    Myoglobin;   

DOI  :  10.1016/0014-5793(91)80495-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown