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Related Experiment Videos

Selenium binding to human hemoglobin via selenotrisulfide.

Mamoru Haratake1, Katsuyoshi Fujimoto, Masahiro Ono

  • 1Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan. haratake@net.nagasaki-u.ac.jp

Biochimica Et Biophysica Acta
|March 23, 2005
PubMed
Summary

A stable selenotrisulfide, PenSSeSPen, reacts with hemoglobin (Hb) in red blood cells (RBCs). Selenium binds to Hb

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Area of Science:

  • Biochemistry
  • Toxicology
  • Redox Biology

Background:

  • Selenotrisulfide is a key intermediate in selenite metabolism.
  • Its reactivity with biological molecules is poorly understood due to instability.
  • Penicillamine forms a stable selenotrisulfide, PenSSeSPen, for study.

Purpose of the Study:

  • Investigate selenite metabolic fate in red blood cells (RBCs).
  • Explore the reaction of stable selenotrisulfide (PenSSeSPen) with human hemoglobin (Hb).

Main Methods:

  • Langmuir binding analysis to quantify selenium binding to Hb.
  • Thiol group blockade using iodoacetamide.
  • MALDI-TOF mass spectrometry to identify selenium binding sites.

Main Results:

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  • PenSSeSPen rapidly reacts with Hb under physiological conditions.
  • Selenium binding correlates with the number of reactive Hb thiol groups.
  • PenSSe moiety binds to beta subunits of Hb, indicating thiol exchange.

Conclusions:

  • PenSSeSPen effectively models selenotrisulfide reactions with Hb.
  • The reaction involves thiol exchange between penicillamine and Hb cysteine residues.
  • This provides insight into selenite metabolism in RBCs.