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

Hemoglobin01:24

Hemoglobin

8.8K
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...
8.8K
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

8.3K
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,...
8.3K
Respiration and Gaseous Exchange01:20

Respiration and Gaseous Exchange

4.2K
The intricate interplay between the cardiovascular and respiratory systems is crucial for efficiently transporting respiratory gases throughout the body. Let us explore the cardiovascular system's multifaceted functions, emphasizing its pivotal role in gas exchange.
Respiration involves the exchange of gases, especially oxygen (O2) and carbon dioxide (CO2), between the alveoli and body cells, a process facilitated by blood circulation. As a result, the cardiovascular system, which involves...
4.2K
Nitric Oxide Signaling Pathway01:28

Nitric Oxide Signaling Pathway

5.3K
Nitric oxide (NO), an inorganic gas, acts as a potent second messenger in most animal and plant tissues. NO diffuses out of the cells that produce it and enters the neighboring cells to generate a downstream response. NO synthase (NOS) catalyzes NO production by the deamination of the amino acid arginine. There are three isoforms of NOS. Endothelial cells have endothelial NOS (eNOS), nerve and muscle cells have neuronal NOS (nNOS), and macrophages produce inducible NOS (iNOS) upon exposure...
5.3K
Protein and Protein Structure02:15

Protein and Protein Structure

72.0K
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...
72.0K
Gene Families01:57

Gene Families

8.0K
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...
8.0K

You might also read

Related Articles

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

Sort by
Same author

Dioxygen and glucose force motion of the electron-transfer switch in the iron(III) flavohemoglobin-type nitric oxide dioxygenase.

Journal of inorganic biochemistry·2023
Same author

Ordered Motions in the Nitric-Oxide Dioxygenase Mechanism of Flavohemoglobin and Assorted Globins with Tightly Coupled Reductases.

Advances in experimental medicine and biology·2022
Same author

Correction: Allostery in the nitric oxide dioxygenase mechanism of flavohemoglobin.

The Journal of biological chemistry·2021
Same author

Allostery in the nitric oxide dioxygenase mechanism of flavohemoglobin.

The Journal of biological chemistry·2020
Same author

Globins Scavenge Sulfur Trioxide Anion Radical.

The Journal of biological chemistry·2015
Same author

Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes.

The Journal of biological chemistry·2010
Same journal

Medicinal Plants and Their Bioactive Phytochemicals as Emerging Therapeutic Strategies for Alzheimer's Disease: An Integrative Review of Preclinical and Clinical Evidence.

Scientifica·2026
Same journal

From Cultivation to Commerce: A Comprehensive Review of the Ecology, Chemistry, Production, Sustainability, and Market Prospects of an Ethiopian Herb Korarima (<i>Aframomum corrorima</i>).

Scientifica·2026
Same journal

Herbal Formula IM-B Possesses Antioxidant Activities and Reduces Expression of Proinflammatory Cytokines in Lipopolysaccharide-Stimulated RAW 264.7 Macrophages.

Scientifica·2026
Same journal

Current Therapeutic Strategies, Recent Advances and the Emerging Potential of Natural Products in Hepatocellular Carcinoma.

Scientifica·2026
Same journal

Local Community Perspectives on the Role of Institutional Stakeholders in Advancing Forest Landscape Restoration in Ghana.

Scientifica·2026
Same journal

Efficiency and Sustainability in Food Supply Chains: A Systematic Analysis.

Scientifica·2026
See all related articles

Related Experiment Video

Updated: May 5, 2026

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

4.4K

Hemoglobin: a nitric-oxide dioxygenase.

Paul R Gardner1

  • 1Miami Valley Biotech, 1001 E. 2nd Street, Suite 2445, Dayton, OH 45402, USA.

Scientifica
|November 27, 2013
PubMed
Summary
This summary is machine-generated.

Nitric oxide dioxygenases (NODs), ancient hemoglobin enzymes, detoxify nitric oxide (NO) and have diverse physiological roles. Research explores their mechanisms, functions, and therapeutic potential in various organisms.

More Related Videos

Application of Genetically Encoded Fluorescent Nitric Oxide (NO&#8226;) Probes, the geNOps, for Real-time Imaging of NO&#8226; Signals in Single Cells
08:32

Application of Genetically Encoded Fluorescent Nitric Oxide (NO•) Probes, the geNOps, for Real-time Imaging of NO• Signals in Single Cells

Published on: March 16, 2017

13.7K
Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

11.4K

Related Experiment Videos

Last Updated: May 5, 2026

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

4.4K
Application of Genetically Encoded Fluorescent Nitric Oxide (NO&#8226;) Probes, the geNOps, for Real-time Imaging of NO&#8226; Signals in Single Cells
08:32

Application of Genetically Encoded Fluorescent Nitric Oxide (NO•) Probes, the geNOps, for Real-time Imaging of NO• Signals in Single Cells

Published on: March 16, 2017

13.7K
Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

11.4K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Hemoglobin superfamily members catalyze nitric oxide dioxygenation, functioning as nitric oxide dioxygenases (NODs).
  • NOD function is an ancient and prevalent role, predating oxygen transport in hemoglobin evolution.
  • Novel NODs are continually discovered across diverse life forms, exhibiting unique structures for varied electron donor interactions.

Purpose of the Study:

  • To elucidate the catalytic mechanism of NODs, including single-domain hemoglobins and multidomain flavohemoglobins.
  • To explore the complex physiological roles of NODs in various biological processes and their involvement with nitric oxide signaling.
  • To investigate the potential therapeutic applications of NODs and their inhibitors.

Main Methods:

  • Characterization of hemoglobin structures and catalytic mechanisms.
  • Utilizing NOD knockout organisms and recombinant NOD-expressing cells for functional studies.
  • Investigating NOD roles in microbial infection, plant senescence, cancer, and metabolic pathways.

Main Results:

  • The NOD catalytic mechanism involves a multistep process including O2 and NO migration, radical coupling, and nitrate release.
  • NODs play critical roles in microbial infection, plant senescence, cancer, mitochondrial function, iron metabolism, and tissue oxygen homeostasis.
  • NOD inhibitors show promise as therapeutic agents, and transgenic NOD applications are being developed for agriculture and industry.

Conclusions:

  • NODs represent a crucial enzymatic function within the hemoglobin superfamily with broad physiological and evolutionary significance.
  • Further research into NOD mechanisms and functions will advance understanding of nitric oxide biology and disease.
  • NODs and their modulators offer promising avenues for therapeutic and biotechnological applications.