Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Oxygen Transport in the Blood

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,...

Hemoglobin

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...

Hypoxia

Hypoxia

Hypoxia is a medical condition characterized by an inadequate oxygen supply to body tissues. It typically manifests as a bluish discoloration of the skin and mucosae, especially in fair-skinned individuals, when hemoglobin (Hb) saturation drops below 75%.
Types of Hypoxia
There are four primary types of hypoxia, each resulting from a different cause:
1. Anemic hypoxia: This type occurs due to insufficient oxygen delivery caused by a lack of red blood cells (RBCs) or RBCs with abnormal or...

Protein and Protein Structure

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...

Nitrosation of Enols

Nitrosation of Enols

The nitrosation reaction is one of the methods of preparing 1,2-diketones. The enol tautomer of the starting ketone reacts with sodium nitrite in hydrochloric acid, generating the 1,2-diketone after hydrolysis.

Respiration and Gaseous Exchange

Respiration and Gaseous Exchange

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 the...

You might also read

Related Articles

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

Sort by

Same author

Contribution of Protein, Starch, and Fiber Composition to the Prediction of Dough Rheology and Baking Quality in U.S. Hard Red Spring Wheat.

Foods (Basel, Switzerland)·2026

Same author

Myoglobin Affects Tissue-Specific Transcriptome, Heart Regeneration and Whole Animal Metabolic Rates.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2026

Same author

STING signals to NF-κB from late endolysosomal compartments using IRF3 as an adaptor.

Nature immunology·2025

Same author

Detection and characterization of a compound 1 species from the <i>c</i>-type heme enzyme cytochrome <i>c</i>'<sub>β</sub>.

Chemical science·2025

Same author

Reactivity of canonical bacterial cytochrome <i>c</i> peroxidases: insights into the electronic structure of compound I.

Chemical science·2025

Same author

Proton-Induced Switching of Paramagnetism: Reversible Conversion between a Low and High Spin Co<sup>III</sup> Center within a Heterobimetallic Core.

Journal of the American Chemical Society·2025

Search research articles

Related Experiment Video

Updated: May 11, 2026

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

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

Published on: February 16, 2022

Oxygen binding to partially nitrosylated hemoglobin.

Angela Fago¹, Alvin L Crumbliss, Michael P Hendrich

¹Department of Bioscience, Aarhus University, DK-8000 Aarhus, Denmark. angela.fago@biology.au.dk

Biochimica Et Biophysica Acta

|April 30, 2013

Summary

Nitric oxide (NO) reactions with hemoglobin (Hb) protect against damage. Partially nitrosylated Hb (Hb-NO) resists oxidation, with its heme geometry and oxygen binding influenced by anions like DPG.

Keywords:

2,3-diphosphoglycerate Allostery DPG EDRF EPR Hb IHP NO Nitric oxide Oxygen binding curve Pentacoordinate S-nitrosated hemoglobin SNO-Hb electron paramagnetic resonance endothelium-derived relaxing factor hemoglobin inositol hexaphosphate nitric oxide

More Related Videos

Detection of Nitric Oxide and Superoxide Radical Anion by Electron Paramagnetic Resonance Spectroscopy from Cells using Spin Traps

Detection of Nitric Oxide and Superoxide Radical Anion by Electron Paramagnetic Resonance Spectroscopy from Cells using Spin Traps

Published on: August 18, 2012

Related Experiment Videos

Last Updated: May 11, 2026

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

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

Published on: February 16, 2022

Detection of Nitric Oxide and Superoxide Radical Anion by Electron Paramagnetic Resonance Spectroscopy from Cells using Spin Traps

Detection of Nitric Oxide and Superoxide Radical Anion by Electron Paramagnetic Resonance Spectroscopy from Cells using Spin Traps

Published on: August 18, 2012

Area of Science:

Biochemistry
Physiology
Spectroscopy

Background:

Nitric oxide (NO) interactions with hemoglobin (Hb) are crucial for mitigating nitrosative damage.
The formation and stability of partially nitrosylated Hb (Hb-NO) remain incompletely understood.
NO depletion in vasculature occurs via oxidation with oxy Hb or binding to deoxy Hb.

Purpose of the Study:

Investigate the interactions between partially nitrosylated Hb and oxygen (O2).
Elucidate the role of NO-heme geometry and anionic effectors on Hb-NO stability and O2 binding.
Clarify the physiological implications of Hb-NO formation for oxygen transport.

Main Methods:

Electron Paramagnetic Resonance (EPR) spectroscopy.
Visible absorption spectroscopy.
Analysis of O2-binding equilibria.

Main Results:

Partially nitrosylated Hb predominantly exhibits hexacoordinate NO-heme geometry and resists O2 oxidation without anions.
Anionic effectors like DPG and IHP promote pentacoordinate heme geometry, increasing Hb-NO oxidation rates.
Anion presence modulates O2 binding, with DPG showing minimal impact on O2-equilibria even with significant NO-heme.
NO-heme formation can destabilize the T-state, reducing O2 affinity, except in the presence of physiological DPG.

Conclusions:

Hb-NO formation and its anion-dependent geometry influence O2 binding.
Physiological conditions with DPG allow NO-mediated protection against nitrosative damage without compromising O2 transport.
These findings highlight a protective mechanism of NO-Hb interactions under physiological conditions.