Heme degradation upon production of endogenous hydrogen peroxide via interaction of hemoglobin with sodium dodecyl sulfate

• The interaction between sodium dodecyl sulfate (SDS) and hemoglobin leads to heme degradation.
• Three compounds suggested by chemometric method in this process.
• Generation of hydrogen peroxide during this process was the reason of heme degradation of hemoglobin.
• Hydrogen peroxide that produced endogenously was more effective than exogenously.
• The endogenous hydrogen peroxide induced aquametHb and hemichrome for hemoglobin.

In this study the hemoglobin heme degradation upon interaction with sodium dodecyl sulfate (SDS) was investigated using UV–vis and fluorescence spectroscopy, multivariate curve resolution analysis, and chemiluminescence method. Our results showed that heme degradation occurred during interaction of hemoglobin with SDS producing three fluorescent components. We showed that the hydrogen peroxide, produced during this interaction, caused heme degradation. In addition, the endogenous hydrogen peroxide was more effective in hemoglobin heme degradation compared to exogenously added hydrogen peroxide. The endogenous form of hydrogen peroxide altered oxyHb to aquamethemoglobin and hemichrome at low concentration. In contrast, the exogenous hydrogen peroxide lacked this ability under same conditions.

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