Related Experiment Video
Updated: Dec 10, 2025

09:43
Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
12.4K
Lessons from the post-genomic era: Globin diversity beyond oxygen binding and transport
Anna Keppner1, Darko Maric1, Miguel Correia1
1Section of Medicine, Department of Endocrinology, Metabolism and Cardiovascular System, University of Fribourg, Fribourg, Switzerland.
Redox Biology
|September 1, 2020
Summary
Vertebrate globins, including hemoglobin and myoglobin, have evolved diverse functions beyond oxygen transport. This review explores their evolutionary journey and varied roles, especially in mammals.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Genomics
Background:
- Hemoglobin (Hb) and myoglobin (Mb) were early protein structure discoveries.
- Genomic data revealed diverse globin types in eukaryotes, bacteria, and some archaea.
- Vertebrates possess additional globin types like neuroglobin (Ngb) and cytoglobin (Cygb).
Purpose of the Study:
- To discuss the evolution of vertebrate globins.
- To highlight the functional diversity of globins, especially non-canonical roles.
- To focus on mammalian globin expression and functions.
Main Methods:
- Literature review of genomic and functional studies on globins.
- Comparative analysis of globin structures and sequences.
- Examination of non-canonical expression sites and functions in mammals.
Main Results:
- Globins exhibit a conserved fold but diverse functions, including NO metabolism and radical scavenging.
- New globin types (Ngb, Cygb, GbE, GbX, GbY, Adgb) have been identified in vertebrates.
- Mammalian globins display atypical functions linked to non-canonical expression sites.
Conclusions:
- Globin evolution showcases remarkable functional adaptation.
- Vertebrate globins have expanded roles beyond oxygen transport.
- Mammalian globins present a paradigm of functional diversification through non-canonical expression.
More Related Videos
Related Concept Videos
Hemoglobin
6.9K
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...
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
6.9K
Oxygen Transport in the Blood
5.3K
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,...
5.3K
Gene Families
9.6K
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.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
9.6K
Globular and Fibrous Proteins
46.4K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
46.4K
Globular and Fibrous Proteins
5.0K
5.0K
Carbon Dioxide Transport in the Blood
3.9K
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...
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...
3.9K

