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

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...
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...
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,...
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...
Structure and Function of Erythrocytes01:29

Structure and Function of Erythrocytes

There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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...

You might also read

Related Articles

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

Sort by
Same author

From Food Additives to Neurodegeneration: The Emerging Role of Polyphosphates in Tauopathies.

ACS chemical neuroscience·2026
Same author

Tirabrutinib-anthracycline interactions in the brain tumor microenvironment: a focus on metabolic inactivation and resistance.

Expert opinion on drug metabolism & toxicology·2025
Same author

Short-chain polyphosphates induce tau fibrillation and neurotoxicity in human iPSC-derived retinal neurons.

Cell death & disease·2025
Same author

Magnetic and MRI Contrast Properties of HumAfFt-SPIONs: Investigating Superparamagnetic Behavior and Enhanced T<sub>2</sub>-Weighted Imaging Performance.

International journal of molecular sciences·2025
Same author

Optical signature of retinal Tau fibrillation.

Scientific reports·2025
Same author

Harnessing macrophage-drug conjugates for allogeneic cell-based therapy of solid tumors via the TRAIN mechanism.

Nature communications·2025

Related Experiment Video

Updated: Jul 6, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

Flavohemoglobin: structure and reactivity.

Alessandra Bonamore1, Alberto Boffi

  • 1Department of Biochemical Sciences, University of Roma La Sapienza, Piazzale Aldo Moro 5, Roma, Italy.

IUBMB Life
|April 2, 2008
PubMed
Summary
This summary is machine-generated.

Flavohemoglobins (flavoHbs) in E. coli, like HMP, scavenge nitric oxide (NO) and reduce it to N2O. They also oxidize NO to nitrate and repair oxidative damage to lipid membranes.

More Related Videos

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
11:51

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Related Experiment Videos

Last Updated: Jul 6, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
11:51

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Area of Science:

  • Biochemistry
  • Microbiology
  • Molecular Biology

Background:

  • Flavohemoglobins (flavoHbs) are bacterial proteins with reductase and oxidase functions.
  • Their roles in oxidative and nitrosative stress response are debated.
  • The Escherichia coli flavoHb (HMP) is a key subject for studying bacterial stress resistance.

Purpose of the Study:

  • To investigate the physiological role of Escherichia coli flavoHb (HMP).
  • To understand HMP's function in bacterial resistance to nitrosative stress.
  • To elucidate HMP's enzymatic activities and potential involvement in cellular protection.

Main Methods:

  • Investigated HMP expression in response to nitric oxide (NO).
  • Examined HMP's NO-scavenging and reduction to N2O under anaerobic conditions.
  • Assessed HMP's NO-oxidation to nitrate (NO-dioxygenase activity) in the presence of O2 and NADH.
  • Evaluated HMP's alkylhydroperoxide reductase activity using NADH.

Main Results:

  • HMP expression is induced by NO in the culture medium.
  • HMP exhibits anaerobic NO-scavenging and reduction to N2O.
  • HMP catalyzes NO oxidation to nitrate in the presence of oxygen.
  • HMP reduces alkylhydroperoxides, suggesting a role in repairing oxidative membrane damage.

Conclusions:

  • HMP plays a crucial role in bacterial defense against nitrosative and oxidative stress.
  • HMP possesses multiple enzymatic activities, including NO detoxification and alkylhydroperoxide reduction.
  • HMP's functions suggest involvement in maintaining cellular integrity during stress conditions.