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

Gene Families01:57

Gene Families

9.5K
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...
9.5K
Protein and Protein Structure02:15

Protein and Protein Structure

84.7K
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.
A protein's shape is critical to its function. For example, an enzyme...
84.7K
Protein Complex Assembly02:41

Protein Complex Assembly

15.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
15.6K
Globular Proteins01:27

Globular Proteins

9.4K
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
9.4K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

46.1K
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...
46.1K
Hemoglobin01:24

Hemoglobin

6.5K
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...
6.5K

You might also read

Related Articles

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

Sort by
Same author

Loading iron(III)porphyrin as the gas/anion binding site into methylated β-cyclodextrin-incorporated polymer hydrogels.

Soft matter·2026
Same author

H<sub>2</sub>O<sub>2</sub> Activation and Alkane Oxidation by Copper Complexes With R-dpa N<sub>3</sub>-Tridentate Ligands: The Complex-Based Dicopper Active Species as a Key Feature in the Efficient Alkane Oxidation.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Singlet-Oxygen-Driven C(sp<sup>2</sup>)-P Bond Cleavage Enables Red-Light Uncaging of Phosphorus(V) Prodrugs on Gold Nanoclusters.

Journal of the American Chemical Society·2026
Same author

N<sub>2</sub> Generation from Nitric Oxide Coordinated to Iron(III) Porphyrin in Acidic Glycine Buffer.

Journal of the American Chemical Society·2025
Same author

CORM-A1 delivers carbon monoxide to the kidney and alleviates post-ischemic renal dysfunction in rat and swine models.

Physiological reports·2025
Same author

Quantification of carbon monoxide (CO) in postmortem human brain tissues after CO poisoning.

Scientific reports·2025

Related Experiment Video

Updated: Nov 24, 2025

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

12.4K

Synthetic heme protein models that function in aqueous solution.

Hiroaki Kitagishi1, Koji Kano

  • 1Department of Molecular Chemistry and Biochemistry, Faculty of Science and Engineering, Doshisha University, 1-3 Tatara Miyakodani, Kyotanabe-city, Kyoto 610-0321, Japan. hkitagis@mail.doshisha.ac.jp kkano@mail.doshisha.ac.jp.

Chemical Communications (Cambridge, England)
|December 21, 2020
PubMed
Summary

Researchers created hemoCD1, an artificial system mimicking myoglobin (Mb) and hemoglobin (Hb) for oxygen (O2) capture. This groundbreaking biomimetic model successfully binds O2 in aqueous solutions, a significant advancement for artificial oxygen carriers.

More Related Videos

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

25.0K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.5K

Related Experiment Videos

Last Updated: Nov 24, 2025

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

12.4K
T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

25.0K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.5K

Area of Science:

  • Biomimetic chemistry
  • Supramolecular chemistry
  • Bioinorganic chemistry

Background:

  • Myoglobin (Mb) efficiently captures molecular oxygen (O2) in aqueous environments.
  • Artificial Mb mimics are challenging due to O2 adduct autoxidation in water.
  • A hydrophobic environment and an electron-donative axial ligand are crucial for O2 binding.

Purpose of the Study:

  • To design and construct a novel artificial system that mimics Mb/hemoglobin (Hb) function.
  • To achieve reversible O2 binding in aqueous solution under physiological conditions.
  • To develop a stable biomimetic model for oxygen transport.

Main Methods:

  • Synthesis of a supramolecular complex termed "hemoCD1".
  • HemoCD1 is a 1:1 inclusion complex of iron(II) porphyrin (FeII TPPS) and a cyclodextrin dimer (Py3CD).
  • Characterization of O2 binding properties in aqueous solution at neutral pH.

Main Results:

  • HemoCD1 demonstrated reversible O2 binding in aqueous solution at neutral pH and ambient temperature.
  • The electronic spectra and functions of hemoCD1 are analogous to natural Mb and Hb.
  • This represents the first artificial Hb/Mb biomimetic model functional in aqueous solution.

Conclusions:

  • HemoCD1 successfully mimics the O2-binding capabilities of Mb and Hb in aqueous media.
  • This work opens avenues for synthesizing hemoCD1 analogues and modeling enzymatic reactions.
  • Potential applications include artificial oxygen carriers and selective toxin removal.