Oxidized dimeric Scapharca inaequivalvis. Co-driven perturbation of the redox equilibrium.

Abstract

The dimeric hemoglobin isolated from Scapharca inaequivalvis, HbI, is notable for its highly cooperative oxygen binding and for the unusual proximity of its heme groups. We now report that the oxidized protein, an equilibrium mixture of a dimeric high spin aquomet form and a monomeric low spin hemichrome, binds ferrocyanide tightly which allows for internal… (More)

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Cite this paper

@article{Boffi1991OxidizedDS, title={Oxidized dimeric Scapharca inaequivalvis. Co-driven perturbation of the redox equilibrium.}, author={Alberto Boffi and Carlo Di Bonaventura and Joseph Bonaventura and Robert E. Cashon and Emilia Chiancone}, journal={The Journal of biological chemistry}, year={1991}, volume={266 27}, pages={17898-903} }