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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Measurement of Heme Synthesis Levels in Mammalian Cells
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Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

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Novel insights into heme binding to hemoglobin.

Marie-Therese Hopp1, Dhruv Chetanbhai Rathod1, Kristina Helena Winn1

  • 1Pharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn, An der Immenburg 4, D-53121 Bonn, Germany.

Biological Chemistry
|August 31, 2022
PubMed
Summary

Human hemoglobin can transiently bind toxic heme through surface motifs, suggesting a potential heme-scavenging role. This interaction may influence hemolysis in diseases like sickle cell disease.

Keywords:
hemeheme-binding motifshemoglobinhemolysismethemoglobin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Hemoglobin and heme release contribute to toxicity in hemolytic diseases like beta-thalassemia and sickle cell disease.
  • Understanding hemoglobin-heme interactions is crucial for disease pathology.

Purpose of the Study:

  • To investigate the transient heme-binding capacity of human hemoglobin via surface-exposed motifs.
  • To characterize the binding affinity and stoichiometry of hemoglobin-heme interactions.
  • To explore the functional consequences of hemoglobin-heme complex formation.

Main Methods:

  • Synthesis and UV-vis spectroscopy of potential heme-binding motifs (HBMs).
  • UV-vis and surface plasmon resonance (SPR) spectroscopy to study hemoglobin-heme binding.
  • In silico molecular docking and simulation studies.
  • Monitoring of peroxidase-like activity of hemoglobin and hemoglobin-heme complexes.

Main Results:

  • Human hemoglobin exhibits transient heme binding through surface motifs with sub- to micromolar affinity.
  • Stoichiometry of binding exceeds a 1:1 ratio, confirmed by in silico studies on the beta-chain.
  • Hemoglobin-heme complexes show significantly enhanced peroxidase-like activity (>1800%).

Conclusions:

  • Human hemoglobin possesses transient heme-binding properties via specific motifs.
  • These interactions suggest a potential heme-scavenging mechanism for hemoglobin.
  • The findings offer new insights into hemoglobin's role in hemolysis and related disease processes.