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Related Concept Videos

Hemoglobin01:24

Hemoglobin

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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.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
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Oxygen Transport in the Blood01:27

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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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Respiration and Gaseous Exchange01:20

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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.
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Gene Families01:57

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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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Gas Exchange and Transport01:20

Gas Exchange and Transport

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Gas exchange, the intake of molecular oxygen (O2) from the environment and the outflow of carbon dioxide (CO2) into the environment, is necessary for cellular function. Gas exchange during respiration occurs largely via the movement of gas molecules along pressure gradients. Gas travels from areas of higher partial pressure to areas of lower partial pressure. In mammals, gas exchange occurs in the alveoli of the lungs, which are adjacent to capillaries and share a membrane with them.
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Protein and Protein Structure02:15

Protein and Protein Structure

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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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Related Experiment Video

Updated: Jan 7, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
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Published on: July 9, 2015

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Hemoglobin as an oxygen gasoreceptor.

Savani Anbalagan1

  • 1Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, Poznań, Poland.

Acta Biochimica Polonica
|January 2, 2026
PubMed
Summary

Hemoglobin may act as an oxygen gasoreceptor, regulating cellular functions beyond gas transport. This discovery could expand the field of gasocrinology to include metabolic gases.

Keywords:
gasocrine signalinggasocrinologygasoreceptorgasotransmitteroxygen receptoroxygen sensingproto-receptorsplit-component signal transduction system

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Hemoglobin primarily transports oxygen and carbon dioxide in vertebrates.
  • Hemoglobin is found in various cell types and organelles, suggesting roles beyond gas transport.
  • Hemoglobin exhibits nitrite reductase activity, producing nitric oxide, a signaling molecule.

Purpose of the Study:

  • To investigate hemoglobin's potential function as a gasoreceptor.
  • To explore hemoglobin's regulatory roles in cellular signaling pathways.
  • To propose hemoglobin as an oxygen proto-gasoreceptor derivative.

Main Methods:

  • Literature review and analysis of hemoglobin's interactions and activities.
  • Hypothesis formulation based on hemoglobin's structure-function relationship.
  • Comparative analysis of hypoxia sensing mechanisms.

Main Results:

  • Hemoglobin interacts with proteins involved in diverse functions, modulated by its oxygen-binding state.
  • Hemoglobin-derived nitric oxide influences vasodilation and mitochondrial respiration.
  • The heme-based domain predates allosteric regions, supporting a proto-gasoreceptor role.

Conclusions:

  • Hemoglobin is proposed as an oxygen gasoreceptor in split-component signal transduction systems.
  • This finding expands the scope of gasocrinology to include metabolic gases.
  • Hemoglobin's diverse roles highlight its significance in cellular regulation.