Aquamethemoglobin reduction by sodium n-dodecyl sulfate via coordinated water oxidation

The influence of sodium n-dodecyl sulfate (SDS) on hemoglobin reduction has been studied in the presence of 100 mM phosphate buffer (pH 7.0) using spectrophotometry, cyclic voltammetry and chemiluminescence (CL) methods. Spectroscopic studies have revealed that the SDS concentration up to 1 mM reduc...

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Bibliographic Details
Published in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2003-07, Vol.30 (1), p.139-146
Main Authors: Moosavi-Movahedi, A.A., Dayer, M.R., Norouzi, P., Shamsipur, M., Yeganeh-faal, A., Chaichi, M.J., Ghourchian, H.O.
Format: Article
Language:English
Subjects:
Chemiluminescence
Cyclic voltammetry
Methemoglobin reduction
SDS
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Summary:The influence of sodium n-dodecyl sulfate (SDS) on hemoglobin reduction has been studied in the presence of 100 mM phosphate buffer (pH 7.0) using spectrophotometry, cyclic voltammetry and chemiluminescence (CL) methods. Spectroscopic studies have revealed that the SDS concentration up to 1 mM reduces the methemoglobin (metHb) to its deoxy form. Such a redox reaction is believed to occur by water oxidation of the sixth coordination in aquametHb. The proposed mechanism is supported by a CL method which monitors H 2O 2 during the conversion of metHb to its deoxy form by addition of SDS at low concentrations (up to 1 mM).
ISSN:0927-7765
1873-4367
DOI:10.1016/S0927-7765(03)00081-X