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

[Hemoglobin, from microorganisms to man: a single structural motif, multiple functions].

Henri Wajcman1, Laurent Kiger

  • 1Inserm U468, hôpital Henri-Mondor, 94010 Créteil, France. Henri.Wajcman@im3.inserm.fr

Comptes Rendus Biologies
|January 11, 2003
PubMed
Summary

Haemoglobins evolved from protecting organisms from toxic gases to oxygen transport. Their diverse functions and structures across species highlight varied evolutionary paths and physiological roles.

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

A Novel Plasma Heme Assay Reveals Disease Severity in Beta-Thalassemia and Sickle Cell Anemia.

American journal of hematology·2026
Same author

Carbon monoxide treatment rescues leukofiltration and preserves storage quality of red blood cell concentrates from sickle cell trait donors.

Transfusion·2026
Same author

An oral carbon monoxide-releasing molecule protects against acute hyperhemolysis in sickle cell disease.

Blood·2024
Same author

A high level of Hb F unmasks a new case of Hb Wanjiang (β (F3-F4) Ala87_Thr88delinsSer_Gln (HBB:c.255_264 delinsTTTTTCTCAG)) in a pregnant woman of African ancestry.

International journal of laboratory hematology·2023
Same author

Preclinical evaluation of the preservation of red blood cell concentrates by hypoxic storage technology for transfusion in sickle cell disease.

Haematologica·2022
Same author

Long-term outcomes of lentiviral gene therapy for the β-hemoglobinopathies: the HGB-205 trial.

Nature medicine·2022

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Context:

  • Haemoglobins (Hbs) are ancient proteins found across diverse life forms, from microorganisms to complex animals.
  • Their structure, characterized by 6-8 helices folding around a heme group, is conserved.
  • Genomic studies trace Hb evolution back 1.8 billion years, coinciding with atmospheric oxygen increase.

Purpose:

  • To explore the evolutionary trajectory of haemoglobin structure and function.
  • To investigate the diverse physiological roles of haemoglobins beyond oxygen transport.
  • To understand the adaptation of haemoglobins in different ecological niches and organisms.

Summary:

  • Microbial haemoglobins, including flavohaemoglobins, truncated haemoglobins, and bacterial haemoglobins, exhibit high oxygen affinity and may have served protective roles.

Related Experiment Videos

  • Plant haemoglobins (non-symbiotic and symbiotic/leghaemoglobins) are involved in energy metabolism and nitrogen fixation.
  • Invertebrate haemoglobins display remarkable diversity in size, structure, and function, including roles in sulfide acquisition and phototrophism, contrasting with the vertebrate tetrameric form.
  • Impact:

    • Reveals the ancient origins and multifaceted evolution of haemoglobin.
    • Highlights the adaptability of haemoglobin to diverse physiological demands, from oxygen scavenging to complex metabolic roles.
    • Underscores the importance of considering functional data alongside structural information for a comprehensive understanding of protein evolution.