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The oxygen binding properties of myo hem erythrin and hem erythrin effect of p mercuri benzoate and per chlorate ion

The oxygen binding properties of myo hem erythrin and hem erythrin effect of p mercuri benzoate and per chlorate ion

Comparative Biochemistry & Physiology A 74(3): 687-692

The O2 binding parameters of hemerythrins from the coelom and muscle of the sipunculid Themiste zostericola were measured. Myohemerythrin had a higher affinity for O2 (P50 [partial pressure of O2 at half saturation] = 1.08 mm Hg, N = 1.02) than did coeleomic hemerythrin (P50 = 3.41 mm Hg, N = 1.13). Covalent chemical modification of 1 cysteine residue in myohemerythrin with p-hydroxymercuribenzoate resulted in a marked increase in O2 affinity (P50 = 0.64 mm Hg). Non-covalent interaction with low concentrations of perchlorate ion had a similar effect (P50 = 0.80 mm Hg). In contrast, low concentrations of perchlorate effected a small decrease in the O2 affinity of the coelomic protein. Perchlorate ion at higher concentrations perturbs the equilibrium between aquomet- and hydroxymethemerythrin, but has no effect on this reaction in myohemerythrin. The sites for binding of perchlorate must therefore be different in these 2 proteins.

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