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Hemoglobin01:24

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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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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,...
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Carbon Dioxide Transport in the Blood01:19

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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.
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The human body utilizes protein buffer systems to maintain a stable pH. These systems capitalize on the dual role of amino acids, which can act as acids or bases by accepting or releasing hydrogen ions in response to pH changes. Protein buffer systems are particularly significant in the extracellular fluid (ECF) and intracellular fluid (ICF) of active cells, where structural and functional proteins provide substantial buffering capacity.
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Carboxyhemoglobin (COHb): Unavoidable Bystander or Protective Player?

André Carrola1, Carlos C Romão2, Helena L A Vieira1,2,3

  • 1UCIBIO, Applied Molecular Biosciences Unit, Department of Chemistry, NOVA School of Science and Technology, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.

Antioxidants (Basel, Switzerland)
|June 28, 2023
PubMed
Summary
This summary is machine-generated.

Carbon monoxide (CO) is a gas with a protective role. Carboxyhemoglobin (COHb), formed from CO, demonstrates cytoprotective and antioxidant functions, suggesting a biological role beyond a simple waste product.

Keywords:
carbon monoxidecarboxyhemoglobincytoprotectionhemoglobinoxidative stress

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Area of Science:

  • Biochemistry
  • Physiology
  • Toxicology

Background:

  • Carbon monoxide (CO) is an endogenous gas produced by heme-oxygenase.
  • CO binds to hemoglobin (Hb) to form carboxyhemoglobin (COHb) in erythrocytes and plasma.
  • COHb has been traditionally viewed as a metabolic byproduct.

Purpose of the Study:

  • To investigate the potential biological role of endogenous carboxyhemoglobin (COHb).
  • To challenge the notion of COHb as merely an innocuous metabolic waste product.
  • To explore COHb's cytoprotective and antioxidant functions.

Main Methods:

  • Literature review of existing data on CO and COHb.
  • Analysis of the correlation between COHb levels and CO toxicity.
  • Examination of COHb's effects in erythrocytes and in vivo hemorrhagic models.

Main Results:

  • No direct correlation was found between carboxyhemoglobin (COHb) levels and carbon monoxide (CO) toxicity.
  • COHb exhibits direct cytoprotective and antioxidant effects within erythrocytes.
  • COHb demonstrates protective benefits in in vivo hemorrhagic models.

Conclusions:

  • Carboxyhemoglobin (COHb) possesses a significant biological role, acting as a cytoprotective and antioxidant molecule.
  • COHb is not merely a waste product but actively contributes to cellular protection.
  • This finding represents a paradigm shift in understanding carbon monoxide (CO) biology, impacting research on CO intoxication and cytoprotection.