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Title
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Control and recognition of anionic ligands in myoglobin.
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Authors
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F.Cutruzzolà,
C.T.Allocatelli,
P.Ascenzi,
M.Bolognesi,
S.G.Sligar,
M.Brunori.
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Ref.
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Febs Lett, 1991,
282,
281-284.
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PubMed id
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Abstract
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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 limacina Mb's, shows that the
introduction of an arginyl residue at the topological position E10 greatly
enhances the stability of the various Mg:heme ligand adducts. Alternative
mechanisms of ligand stabilization may therefore be operative in Mb's lacking
the distal histidine.
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