Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Electron transfer kinetics between hemoglobin subunits.

L Kiger1, M C Marden

  • 1INSERM U 473, 84, rue du Général Leclerc, 94276 Le Kremlin-Bicêtre, France.

The Journal of Biological Chemistry
|October 17, 2001
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

[SaO<sub>2</sub> and PaO<sub>2</sub> mismatch: Do not forget hemoglobinopathy].

Revue des maladies respiratoires·2018
Same author

Asymmetry of calmodulin revealed by peptide binding.

Journal of fluorescence·2013
Same author

Heme binds to factor VIII and inhibits its interaction with activated factor IX.

Journal of thrombosis and haemostasis : JTH·2012
Same author

A new generation of polymer nanoparticles for drug delivery.

Cellular and molecular biology (Noisy-le-Grand, France)·2004
Same author

Short insertion in a hemoglobin chain: Hb Esch, an unstable alpha1 variant with duplication of the sequence Ala65-Leu-Thr-Asn68.

Blood cells, molecules & diseases·2003
Same author

Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family.

The Journal of biological chemistry·2001
Same journal

Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

The Journal of biological chemistry·2026
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
See all related articles

Electron transfer in hemoglobin (Hb) hybrids shows a faster rate from alpha to beta subunits under anaerobic conditions. This process, crucial for methemoglobin distribution in red blood cells, occurs via inter-tetramer collisions.

Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Molecular Biology

Background:

  • Hemoglobin (Hb) is a tetrameric protein responsible for oxygen transport.
  • Valency hybrids of Hb, with subunits in different oxidation states, are crucial for understanding electron transfer dynamics.
  • Methemoglobin formation and reduction are vital processes within erythrocytes.

Purpose of the Study:

  • To investigate the kinetics of electron transfer in hemoglobin valency hybrids.
  • To determine the directionality and mechanism of electron transfer between Hb subunits.
  • To elucidate the role of Hb quaternary structure and inter-tetramer interactions in electron transfer.

Main Methods:

  • Measurement of electron transfer kinetics in Hb valency hybrids under anaerobic and oxygenated conditions.

Related Experiment Videos

  • Incubation of Hb samples at specific pH and temperature to observe subunit oxidation state changes.
  • Utilizing cross-linked tetramer Hb A and deoxy Hb S to study inter-tetramer electron transfer.

    • Main Results:

    • Electron transfer was observed predominantly between deoxy and aquo-met subunits (high spin species).
    • A faster electron transfer rate was measured in the direction of alpha to beta subunits (a few hours at pH 7, 25°C).
    • Electron transfer kinetics were independent of Hb quaternary state and occurred via inter-tetramer collisions, dependent on Hb concentration.

    Conclusions:

    • Electron transfer in Hb hybrids is primarily driven by collisions between tetramers.
    • The findings suggest a mechanism for methemoglobin distribution within erythrocytes involving Hb tetramer interactions.
    • In vivo, Hb tetramer collisions likely play a significant role in methemoglobin distribution alongside erythrocyte reductase systems.