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

Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.0K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
8.0K
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

12.5K
The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...
12.5K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

15.0K
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
15.0K
Oxidation and Reduction of Organic Molecules01:19

Oxidation and Reduction of Organic Molecules

7.5K
Energy production within a cell involves many coordinated chemical pathways. Most of these pathways are combinations of oxidation and reduction reactions, which occur at the same time. An oxidation reaction strips an electron from an atom in a compound, and the addition of this electron to another compound is a reduction reaction. Because oxidation and reduction usually occur together, these pairs of reactions are called redox reactions.
The removal of an electron from a molecule, results in a...
7.5K
Redox Reactions01:27

Redox Reactions

185
Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
185
Electron Transport Chains01:28

Electron Transport Chains

102.6K
The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
102.6K

You might also read

Related Articles

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

Sort by
Same author

Causal links between diabetes, gut microbiota, and colon cancer: insights from Mendelian randomization.

Endokrynologia Polska·2026
Same author

Toward smart health monitoring: multimodal sensing and intelligent disease diagnosis in poultry and livestock.

Animal frontiers : the review magazine of animal agriculture·2026
Same author

Immobilized neuroglobin scavenges carbon monoxide from circulating carboxyhemoglobin.

bioRxiv : the preprint server for biology·2026
Same author

Expansion of stemlike HIV-specific CD8<sup>+</sup> T cells and limited viral epitope diversity characterize durable posttreatment control of HIV.

Science translational medicine·2026
Same author

Distinct polyp recurrence timing and STK11 mutation status underlie clinical heterogeneity in pediatric Peutz-Jeghers syndrome.

Journal of pediatric gastroenterology and nutrition·2026
Same author

Structural basis of mpox virus A30/H2 subcomplex formation.

Proceedings of the National Academy of Sciences of the United States of America·2026

Related Experiment Video

Updated: Sep 11, 2025

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.0K

Cytochrome b 5 reductase 4 efficiently reduces Neuroglobin and Cytoglobin.

Anthony W DeMartino1, Onaje Cunningham1, Saumika Mulluri1

  • 1Heart, Lung, Blood and Vascular Medicine Institute, University of Pittsburgh, Pittsburgh, PA 15261.

Biorxiv : the Preprint Server for Biology
|August 12, 2025
PubMed
Summary
This summary is machine-generated.

Cytochrome b5 reductase 4 efficiently reduces both cytoglobin and neuroglobin, a protein previously lacking a known reductase. This finding suggests a key role for this enzyme in maintaining the ferrous state of these important heme proteins in vivo.

Keywords:
Cytochrome b5 reductase 3Cytochrome b5 reductase 4CytoglobinNeuroglobin

More Related Videos

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

12.2K
Unveiling Xenobiotic Transport and Effects in Isolated Mitochondria: Insights from Respirometric and Enzymatic Assays
08:03

Unveiling Xenobiotic Transport and Effects in Isolated Mitochondria: Insights from Respirometric and Enzymatic Assays

Published on: March 7, 2025

695

Related Experiment Videos

Last Updated: Sep 11, 2025

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.0K
Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

12.2K
Unveiling Xenobiotic Transport and Effects in Isolated Mitochondria: Insights from Respirometric and Enzymatic Assays
08:03

Unveiling Xenobiotic Transport and Effects in Isolated Mitochondria: Insights from Respirometric and Enzymatic Assays

Published on: March 7, 2025

695

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Cytoglobin and neuroglobin are heme-containing proteins with incompletely defined physiological roles.
  • Their functions often depend on the heme iron being in the ferrous (Fe2+) state, necessitating cellular reducing systems.
  • The cytochrome b5 reductase 3/cytochrome b5 system reduces cytoglobin but not neuroglobin.

Purpose of the Study:

  • To investigate the interaction of cytochrome b5 reductase 4 (CBR4) with cytoglobin and neuroglobin.
  • To identify potential physiological reducing systems for neuroglobin.
  • To explore the impact of specific protein mutations on reduction rates.

Main Methods:

  • Enzymatic assays measuring the reduction rates of cytoglobin and neuroglobin by CBR4.
  • Site-directed mutagenesis of surface residues on cytoglobin and neuroglobin.
  • Comparison of reduction rates for wild-type and mutant proteins.

Main Results:

  • CBR4 efficiently reduces both cytoglobin and neuroglobin.
  • CBR4 reduces cytoglobin at rates comparable to the CBR3/cytochrome b5 system.
  • Specific cytoglobin mutations (R84E, K116E) significantly decreased reduction rates, while neuroglobin mutations affecting cytochrome c interaction had minimal impact on CBR4 reduction.

Conclusions:

  • CBR4 is a strong candidate for the physiological reduction of neuroglobin.
  • CBR4 can supplement the role of CBR3/cytochrome b5 in cytoglobin reduction in vivo.
  • Distinct surface residues influence the interaction of cytoglobin and neuroglobin with their respective reductases.