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Control and recognition of anionic ligands in myoglobin
Author(s) -
Cutruzzolà Francesca,
Allocatelli Carlo Travaglini,
Ascenzi Paolo,
Bolognesi Martino,
Sligar Stephen G.,
Brunori Maurizio
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80495-o
Subject(s) - myoglobin , chemistry , biochemistry
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.