Abstract
Interactions of two anionic surfactants, sodium dodecyl sulphate (SDS) and sodium bis(2-ethylhexyl) sulfosuccinate (AOT) at concentrations below and above critical micelle concentration with methemoglobin (metHb) have been investigated by conventional as well as by stopped-flow absorption and fluorescence spectroscopy. The absorption spectra of metHb in AOT reverse micelles have been also analyzed. Both surfactants in their monomeric form convert metHb to reversible hemichrome. This is connected with a diminution of peroxidase-like activity of metHb and with an increase of the susceptibility of heme for a damage by H2O2. In micellar solutions of AOT and SDS as well as in AOT reverse micelles pentacoordinated ferric species seems to be the predominant form of this protein. It has been concluded, basing on a kinetic analysis, that conformational changes in the heme environment of metHb as induced by both surfactants occur independently of the alterations in the tertiary structure of this protein.
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