PMID: 11904230Mar 21, 2002Paper

The effect of anions on azide binding to myoglobin: an unusual functional modulation

Biochimica Et Biophysica Acta
M Cristina De RosaAndrea Brancaccio

Abstract

The effect of increasing concentrations of several anions on the azide (N(-)(3)) binding properties of sperm whale and horse ferric myoglobin has been studied. Surprisingly, a number of anions may act as heterotropic effectors, decreasing the affinity of myoglobins for N(-)(3), in the following order: ClO(-)(4)=I(-)>Br(-)>Cl(-) and SO(2-)(4), which mirrors the increase in their charge density. The largest effects were measured using ClO(-)(4) and I(-), which produce a 4-fold and 8-fold reduction of the N(-)(3) binding affinity in horse and sperm whale myoglobins, respectively. A dissociation equilibrium constant (K(d)) ranging from 150 to 250 mM was estimated for ClO(-)(4) and I(-) binding to myoglobins. In order to analyse the molecular mechanism producing the reduction of the N(-)(3) binding affinity to ferric myoglobin, the potential anionic binding sites within ferric myoglobin were investigated by a molecular modelling study using the program Grid. Analysis of the theoretical results suggests two particularly favourable binding sites: the first, next to the distal side of the haem, whose occupancy might alter the electrostatic potential surrounding the bound N(-)(3); the second, involving residues of helices B and G which ...Continue Reading

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Feb 2, 2008·Methods in Enzymology·Benoit J SmaggheMark S Hargrove
Jul 21, 2004·Clinical Chemistry and Laboratory Medicine : CCLM·Enrico Di StasioLeopoldo Paolo Pucillo
Dec 22, 2020·Chemical Communications : Chem Comm·Hiroaki Kitagishi, Koji Kano

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