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

Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
Gene Families01:57

Gene Families

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Hemoglobin01:24

Hemoglobin

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...
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

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,...

You might also read

Related Articles

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

Sort by
Same author

The Role of the <i>Pseudomonas aeruginosa</i> Heme Metabolites Biliverdin IXβ and IXδ in Pathogenesis and Infection.

Journal of the American Society for Mass Spectrometry·2026
Same author

PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa.

The Journal of biological chemistry·2026
Same author

Heme Trafficking and the Importance of Handling Nature's Most Versatile Cofactor.

Chemical reviews·2025
Same author

Mechanisms of bacterial heme uptake and degradation: Diverse strategies for ring opening.

Journal of inorganic biochemistry·2025
Same author

GaSal-2: A Water-Soluble Antipseudomonal Agent Targeting the Extracellular Hemophore HasAp.

ACS infectious diseases·2025
Same author

Application of preclinical absorption, distribution, metabolism, elimination in vitro techniques for the characterization and compound library optimization of novel antibiotic gallium salophen.

Drug metabolism and disposition: the biological fate of chemicals·2025
Same journal

Inflammation Impairs Poststroke Recovery by Disrupting Iron Homeostasis in Brain.

Antioxidants & redox signaling·2026
Same journal

Histone Lactylation Links Glycolysis to Ferroptosis in Diabetic Cataract.

Antioxidants & redox signaling·2026
Same journal

Insights into the Multifaceted Roles of 3-Mercaptopyruvate Sulfurtransferase in Liver Diseases.

Antioxidants & redox signaling·2026
Same journal

NINJ1 Aggravates Doxorubicin-Induced Cardiotoxicity by Suppressing AMPK-Mediated HIF-1α Deubiquitination.

Antioxidants & redox signaling·2026
Same journal

<i>Corrigendum to:</i> Suppression of Cardiac Autophagy by Hyperinsulinemia in Insulin Receptor-Deficient Hearts Is Mediated by Insulin-Like Growth Factor Receptor Signaling.

Antioxidants & redox signaling·2026
Same journal

Sleeve Gastrectomy Is Associated with Improved Systemic Redox Homeostasis in T2DM Through Ghrelin-GHSR Attenuation, POMC Neuronal Modulation, and CD4<sup>+</sup> T Cell Metabolic Reprogramming.

Antioxidants & redox signaling·2026
See all related articles

Related Experiment Video

Updated: Jul 1, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Heme oxygenase: evolution, structure, and mechanism.

Angela Wilks1

  • 1Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD 21201-1180, USA. awilks@rx.maryland.edu

Antioxidants & Redox Signaling
|September 17, 2002
PubMed
Summary
This summary is machine-generated.

Heme oxygenase enzymes catalyze essential heme breakdown across diverse life forms. This review explores their conserved structure and function, crucial for iron metabolism and more.

More Related Videos

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Related Experiment Videos

Last Updated: Jul 1, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • Heme oxygenase (HO) catalyzes the oxidative cleavage of heme, a vital reaction in diverse physiological processes.
  • These processes include iron reutilization, cellular signaling, pigment synthesis, and bacterial iron acquisition.
  • HO shares a conserved structural and mechanistic scaffold despite its varied roles.

Purpose of the Study:

  • To review the evolution of structural and functional properties of heme oxygenase.
  • To integrate recent crystal structure data of mammalian and bacterial enzymes.

Main Methods:

  • Comparative analysis of heme oxygenase structures.
  • Review of existing literature on heme oxygenase function and evolution.

Main Results:

  • Heme oxygenase exhibits a conserved scaffold across diverse organisms and functions.
  • The enzyme's catalytic mechanism is distinct from other hemoproteins but utilizes a shared hemoprotein scaffold.
  • Recent crystal structures provide insights into evolutionary adaptations.

Conclusions:

  • Heme oxygenase represents a highly evolved enzyme with conserved structural and functional characteristics.
  • Understanding HO evolution is key to appreciating its diverse physiological roles.
  • Structural insights are crucial for deciphering HO's evolutionary trajectory.