Sulfhemoglobin under the spotlight – Detection and characterization of SHb and HbFeIII–SH

Sulfhemoglobinemia is an incurable disease caused by an overdose of sulfur-containing drugs with oxidizing properties. Its diagnosis remains hindered due to the similarity of symptoms to other pathological state – methemoglobinemia, as well as contradictory information on the structure and character...

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Published in:Biochimica et biophysica acta. Molecular cell research 2023-01, Vol.1870 (1), p.119378-119378, Article 119378
Main Authors: Stepanenko, Tetiana, Zając, Grzegorz, Czajkowski, Artur, Rutkowska, Wiktoria, Górecki, Andrzej, Marzec, Katarzyna Maria, Dybas, Jakub
Format: Article
Language:English
Subjects:
Hemoglobin
Human erythrocytes
Molecular spectroscopy
Raman spectroscopy
Red blood cells
Sulfhemoglobinemia
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Summary:Sulfhemoglobinemia is an incurable disease caused by an overdose of sulfur-containing drugs with oxidizing properties. Its diagnosis remains hindered due to the similarity of symptoms to other pathological state – methemoglobinemia, as well as contradictory information on the structure and characteristics of sulfhemoglobin. Herein, we present sulfhemoglobinemia model on living functional human erythrocytes, designed to recreate processes which could take place in a patient body in order to complement missing information and highlight distinctiveness of two hemoglobin (Hb) adducts formed after interaction with sulfur donors. Employed techniques, UV–Vis absorption, Raman, Fourier transformed infrared (FT–IR) and electronic circular dichroism (ECD) spectroscopies, allowed to distinguish and characterize Hb adduct with sulfur atom bounded directly to the iron ion (HbFeIII–SH), and irreversibly connected to the porphyrin ring (SHb – sulfhemoglobin). Presented herein results provided also new evidence on formation of both these hemoglobin adducts inside functional erythrocytes under oxidative conditions and during sulfur-containing drug presence, what can be further translated into future physiological studies. Moreover, we found that sulfur attachment to the porphyrin ring altered Hb structure and lead to changes in protein packing inside RBCs, eventually. Interestingly, measurement of blood drop smear by Raman spectroscopy occurred the most accurate method to differentiate HbFeIII–SH and SHb, indicating potential of this technique in sulfhemoglobinemia diagnosis. •Sulfur-containing drugs promote formation of two distinct types of hemoglobin (Hb) adducts.•Sulfur can bind to the porphyrin ring (SHb) or to the ferric iron ion (HbFeIII–SH).•Raman spectroscopy enables differentiation between SHb and HbFeIII–SH.•Attachment of sulfur to the porphyrin ring alters Hb packing inside red blood cells.
ISSN:0167-4889
1879-2596
DOI:10.1016/j.bbamcr.2022.119378