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J Photochem Photobiol B. 2014 Apr 5;133:11-7. doi: 10.1016/j.jphotobiol.2014.02.014. Epub 2014 Mar 6.

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

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Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran. Electronic address:
Departments of Ophthalmology and Visual Sciences and Pharmacology, University of Wisconsin School of Medicine and Public Health, Madison, WI, USA.
Schools of Biology, University of Tehran, Tehran, Iran.


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.


Chemiluminescence; Endogenous hydrogen peroxide; Heme degradation; Hemoglobin; Multivariate curve resolution; Sodium dodecyl sulfate

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