Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

5.2K
Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
5.2K
Hemoglobin01:24

Hemoglobin

9.9K
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...
9.9K
Lifecycle of Erythrocytes01:22

Lifecycle of Erythrocytes

6.0K
Erythrocytes, also known as red blood cells, constantly move through blood capillaries. As a result, they damage their plasma membrane due to the continuous friction. Typically, after 100 to 120 days, erythrocytes become rigid and fragile as they wear out. As they pass through small vessels in the spleen and liver, they can get trapped and break apart into fragments.
The resident phagocytic macrophages deal with these damaged cells by engulfing them and separating their globin and heme groups....
6.0K
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

8.4K
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,...
8.4K
Metal-Ligand Bonds02:51

Metal-Ligand Bonds

25.6K
The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
25.6K
Microbes and Other Elemental Cycles01:24

Microbes and Other Elemental Cycles

66
Microbial activity plays a pivotal role in the biogeochemical cycling of iron and manganese, especially at the redox gradients characteristic of stratified aquatic environments. These cycles are driven by microbial transformations between oxidized and reduced forms of the metals, allowing organisms to exploit them for metabolic energy and structural purposes.Iron Cycling Across Redox GradientsIn neutral, oxygen-rich surface waters, iron is predominantly found in its oxidized, insoluble ferric...
66

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Recent Trends in Metabolomics by NMR Spectroscopy.

Angewandte Chemie (International ed. in English)·2026
Same author

Structural biology of ferritin nanocages.

FEBS letters·2026
Same author

An Integrated NMR Approach for Evaluating Linker-Payload Conjugation with Monoclonal Antibodies.

Bioconjugate chemistry·2026
Same author

S1P<sub>3</sub> Receptor Mediates the Proinflammatory Effect of the Endocannabinoid 2-Arachidonoylglycerol in Endometriotic Epithelial Cells.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2025
Same author

Ferritin-assisted biomineralization and drug delivery: It's a matter of hard and soft.

Journal of inorganic biochemistry·2025
Same author

Design of 2-Aminobenzothiazole Derivatives Targeting Trypanosomatid PTR1 by a Multidisciplinary Fragment Hybridization Approach.

Journal of medicinal chemistry·2025

Related Experiment Video

Updated: Apr 4, 2026

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells
10:23

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

10.6K

Iron binding to human heavy-chain ferritin.

Cecilia Pozzi1, Flavio Di Pisa1, Caterina Bernacchioni2

  • 1Dipartimento di Biotecnologie, Chimica e Farmacia, Università di Siena, Via Aldo Moro 2, 53100 Siena, Italy.

Acta Crystallographica. Section D, Biological Crystallography
|September 2, 2015
PubMed
Summary

Maxi-ferritins store iron using a cage structure. Researchers mapped iron

Keywords:
ferritinhuman heavy chainironmechanism

More Related Videos

Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes
08:45

Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes

Published on: May 10, 2022

2.6K
Assessing Iron Deposition in the Brains of 5xFAD Mice by Perls'/DAB Staining
07:32

Assessing Iron Deposition in the Brains of 5xFAD Mice by Perls'/DAB Staining

Published on: May 23, 2025

1.5K

Related Experiment Videos

Last Updated: Apr 4, 2026

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells
10:23

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

10.6K
Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes
08:45

Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes

Published on: May 10, 2022

2.6K
Assessing Iron Deposition in the Brains of 5xFAD Mice by Perls'/DAB Staining
07:32

Assessing Iron Deposition in the Brains of 5xFAD Mice by Perls'/DAB Staining

Published on: May 23, 2025

1.5K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biomineralization

Background:

  • Maxi-ferritins are essential iron-storage proteins composed of 24 subunits forming a cage.
  • Iron biomineralization is facilitated by catalytic iron(II) oxidation at oxidoreductase sites (OS).
  • Human H ferritin and Rana catesbeiana M protein are vertebrate maxi-ferritins with known structures.

Purpose of the Study:

  • To elucidate the iron pathway within human H ferritin at high resolution.
  • To comparatively analyze iron-binding sites in human H ferritin and R. catesbeiana M protein.
  • To understand how differences in iron-binding sites influence ferritin activity.

Main Methods:

  • High-resolution crystal structure determination of iron-bound human H ferritin.
  • Time-resolved cryo-crystallography after ferrous salt exposure.
  • Comparative structural analysis of iron sites.
  • Stopped-flow kinetics assays.

Main Results:

  • Identified multiple binding sites detailing the iron path from entry channels to OS.
  • Revealed distinct patterns of ligands defining pre-OS iron sites in human H ferritin versus R. catesbeiana M protein.
  • Demonstrated differential catalytic activity between human H ferritin and R. catesbeiana M protein.

Conclusions:

  • The structural and kinetic data provide insights into the mechanism of iron biomineralization.
  • Differences in transient iron-binding sites correlate with observed species-specific variations in ferritin activity.
  • This study enhances our understanding of ferritin's role in iron homeostasis and disease.