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Related Concept Videos

Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
Hemoglobin01:24

Hemoglobin

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.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Hypoxia01:23

Hypoxia

Hypoxia is a medical condition characterized by an inadequate oxygen supply to body tissues. It typically manifests as a bluish discoloration of the skin and mucosae, especially in fair-skinned individuals, when hemoglobin (Hb) saturation drops below 75%.
Types of Hypoxia
There are four primary types of hypoxia, each resulting from a different cause:
1. Anemic hypoxia: This type occurs due to insufficient oxygen delivery caused by a lack of red blood cells (RBCs) or RBCs with abnormal or...
Respiration and Gaseous Exchange01:20

Respiration and Gaseous Exchange

The intricate interplay between the cardiovascular and respiratory systems is crucial for efficiently transporting respiratory gases throughout the body. Let us explore the cardiovascular system's multifaceted functions, emphasizing its pivotal role in gas exchange.
Respiration involves the exchange of gases, especially oxygen (O2) and carbon dioxide (CO2), between the alveoli and body cells, a process facilitated by blood circulation. As a result, the cardiovascular system, which involves the...
Ions, Molecules, and Compounds01:23

Ions, Molecules, and Compounds

Ions - When an atom participates in a chemical reaction that results in the donation or acceptance of one or more electrons, the atom becomes positively or negatively charged. This frequently happens for most atoms to have a full valence shell. This can happen either by gaining electrons to fill a shell that is more than half-full or by giving away electrons to empty a shell that is less than half-full, thereby leaving the next smaller electron shell as the new, full valence shell. An atom with...
Carbon Dioxide Transport in the Blood01:19

Carbon Dioxide Transport in the Blood

Carbon dioxide (CO2) transport in the blood is critical to human physiology. On average, our body cells produce around 200 mL of CO2 per minute, precisely the quantity expelled by the lungs. This process involves the transportation of CO2 from the tissue cells to the lungs in three primary forms.
Forms of CO2 Transport
1. Dissolved in plasma: A small percentage (7-10%) of CO2 is transported and dissolved directly in the plasma.
2. Carbaminohemoglobin: Just over 20% of CO2 is chemically bound to...

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Related Experiment Video

Updated: Jul 7, 2026

Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications
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Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications

Published on: May 8, 2026

An alternative theoretical formula for hemoglobin oxygenation.

Denis Michel1

  • 1Molecular and Cellular Interactions, Université de Rennes 1, CNRS UMR6026 Hip IFR140, Campus de Beaulieu. Bat. 13, 35042, Rennes Cedex, France. denis.michel@univ-rennes1.fr

European Biophysics Journal : EBJ
|February 21, 2008
PubMed
Summary

Human hemoglobin oxygenation may not rely on affinity changes. Evidence suggests subunits are not equally available for oxygen binding, challenging traditional allostery models.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • Classical models of homotropic allostery assume equivalent binding sites.
  • Hemoglobin's oxygen binding is crucial for oxygen transport.
  • Existing models do not fully explain hemoglobin's complex oxygenation behavior.

Purpose of the Study:

  • To investigate the mechanism of human hemoglobin oxygenation.
  • To challenge the postulate of equivalent binding sites in allosteric models.
  • To explore an alternative mechanism for hemoglobin oxygenation.

Main Methods:

  • Analysis of existing evidence on subunit availability.
  • Incorporation of findings into the Adair scheme.
  • Re-evaluation of classical allosteric models.

Main Results:

  • Human hemoglobin subunits are not simultaneously available for oxygen equilibration.
  • This subunit unavailability reduces the number of possible intermediate microstates.
  • The Adair scheme, modified with these findings, suggests a new oxygenation mechanism.

Conclusions:

  • Human hemoglobin oxygenation may occur through a mechanism independent of affinity changes.
  • The assumption of equivalent binding sites in allosteric models may be flawed for hemoglobin.
  • This study offers a novel perspective on hemoglobin's allosteric regulation.