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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.
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Related Experiment Video

Updated: May 29, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

A membrane-bound vertebrate globin.

Miriam Blank¹, Jessica Wollberg, Frank Gerlach

¹Biocenter Grindel, University of Hamburg, Hamburg, Germany.

|September 28, 2011

Summary

Zebrafish globin X, a unique vertebrate protein, is localized to the cell membrane, requiring myristoylation and palmitoylation for targeting. This membrane-associated globin may protect lipids or function in redox signaling.

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Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Vertebrate globins, including hemoglobin and myoglobin, are known for oxygen binding.
Globin X, found in fish and amphibians, has unclear functions and is expressed in the zebrafish central nervous system.
Globin X possesses a unique N-terminal extension with potential membrane-association sites.

Purpose of the Study:

To investigate the intracellular localization and membrane association of zebrafish globin X.
To determine the role of N-myristoylation and S-palmitoylation sites in globin X targeting.
To characterize the oxygen-binding properties of globin X.

Main Methods:

Utilized green fluorescence protein (GFP) fusion constructs to study globin X localization in 3T3 cells.
Mutagenesis of putative N-myristoylation and S-palmitoylation sites.
Oxygen binding assays to determine affinity and cooperativity.

Main Results:

Zebrafish globin X requires both N-myristoylation and S-palmitoylation for correct targeting and membrane localization.
This study identifies globin X as the first vertebrate globin found as a component of the cell membrane.
Globin X exhibits hexacoordinate binding and cooperative oxygen binding with variable affinity.

Conclusions:

Globin X is a membrane-associated protein, distinct from canonical intracellular globins.
Its function is unlikely to be respiratory; it may protect cell membranes from oxidation or act as a redox sensor.
The findings open new avenues for understanding the diverse roles of globins in vertebrates.