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Related Experiment Videos

Structural model for the trialkyltin binding site on cat hemoglobin.

A L Chu1, F Taketa, A G Mauk

  • 1Department of Biochemistry, University of British Columbia, Vancouver, Canada.

Journal of Biomolecular Structure & Dynamics
|December 1, 1985
PubMed
Summary
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Trialkyltin complexes preferentially bind to R-state cat hemoglobin. This binding involves specific atoms on cysteine and histidine residues, with interactions changing upon deoxygenation.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Toxicology

Background:

  • Trialkyltin compounds exhibit known in vivo metabolic effects.
  • Understanding their molecular interactions is crucial for toxicology and drug development.
  • Hemoglobin serves as a model system for studying protein-ligand interactions.

Purpose of the Study:

  • To elucidate the binding site and mechanism of trialkyltin complexes on cat oxyhemoglobin.
  • To investigate the conformational changes in hemoglobin upon deoxygenation affecting ligand binding.
  • To propose a model for trialkyltin interactions with enzymes based on hemoglobin binding.

Main Methods:

  • Computational modeling and structural analysis of hemoglobin.
  • Characterization of ligand binding sites.

Related Experiment Videos

  • Comparative analysis of oxygenated and deoxygenated hemoglobin states.

    • Main Results:

    • The binding site for trialkyltin complexes on alpha-chain cat oxyhemoglobin involves Cys-13 (SG atom) and His-113 (NE2 atom).
    • Deoxygenation induces conformational changes, restricting trialkyltin binding to His-113 (ND1 nitrogen), a less favorable interaction.
    • This explains the preferential binding to the R-state (oxygenated) hemoglobin.

    Conclusions:

    • A model is presented explaining preferential trialkyltin binding to R-state hemoglobin.
    • The findings suggest the nature of trialkyltin interactions with various enzymes.
    • This research aids in understanding the in vivo metabolic effects of trialkyltin compounds.