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

Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

105
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
105
Biosynthesis of Nucleic Acids01:28

Biosynthesis of Nucleic Acids

154
Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...
154
Drug Metabolism: Phase I Reactions01:17

Drug Metabolism: Phase I Reactions

3.5K
A phase I reaction is a biochemical process that introduces a functionally reactive polar group to a substance. This transformation predominantly occurs in the liver, facilitated by the cytochrome P450 system of hemoproteins situated in the lipophilic endoplasmic reticulum of cells. The metabolite generated through this process can have varying polarities. If it is sufficiently polar, it can be easily excreted in the urine due to its water compatibility. However, if the metabolite is nonpolar,...
3.5K
Peroxisomes01:24

Peroxisomes

13.9K
Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
13.9K
Phase I Reactions: Oxidation of Aliphatic and Aromatic Carbon-Containing Systems01:19

Phase I Reactions: Oxidation of Aliphatic and Aromatic Carbon-Containing Systems

302
Phase I biotransformation reactions are integral to drug metabolism, predominantly involving oxidative, reductive, and hydrolytic transformations. Chief among these are oxidative reactions, which enhance the hydrophilicity of xenobiotics and introduce polar functional groups to facilitate their elimination from the body.
Oxidation reactions are fundamental in aromatic carbon-containing systems. An example is the hydroxylation of phenobarbital, a process that transforms it into...
302
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

3.6K
Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
3.6K

You might also read

Related Articles

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

Sort by
Same author

The terminal heme synthetic enzyme, coproheme decarboxylase, negatively regulates heme uptake in Mycobacterium tuberculosis.

The Journal of biological chemistry·2026
Same author

Direct Spectroscopic Ferrochelatase Assay.

Methods in molecular biology (Clifton, N.J.)·2024
Same author

Impact of Phosphorylation at Various Sites on the Active Pocket of Human Ferrochelatase: Insights from Molecular Dynamics Simulations.

International journal of molecular sciences·2024
Same author

The alternative coproporphyrinogen III oxidase (CgoN) catalyzes the oxygen-independent conversion of coproporphyrinogen III into coproporphyrin III.

Frontiers in microbiology·2024
Same author

Exploiting Differences in Heme Biosynthesis between Bacterial Species to Screen for Novel Antimicrobials.

Biomolecules·2023
Same author

Exploring Academic Performance of Medical Students in an Integrated Hybrid Curriculum by Gender.

Medical science educator·2023

Related Experiment Video

Updated: Aug 30, 2025

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

A primer on heme biosynthesis.

Harry A Dailey1,2, Amy E Medlock1,3

  • 1Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-1111, USA.

Biological Chemistry
|August 27, 2022
PubMed
Summary

Heme biosynthesis involves three distinct pathways: siroheme-dependent, coproporphyrin-dependent, and protoporphyrin-dependent. This review details these heme synthesis routes and their regulation.

Keywords:
coproporphyrin dependent pathwayhememitochondrial heme metabolonporphyriaprotoporphyrin dependent pathwaysiroheme dependent pathway

More Related Videos

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
05:17

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

Published on: July 28, 2016

10.4K
Stimulation of Stem Cell Niches and Tissue Regeneration in Mouse Skin by Switchable Protoporphyrin IX-Dependent Photogeneration of Reactive Oxygen Species In Situ
10:05

Stimulation of Stem Cell Niches and Tissue Regeneration in Mouse Skin by Switchable Protoporphyrin IX-Dependent Photogeneration of Reactive Oxygen Species In Situ

Published on: May 8, 2020

2.0K

Related Experiment Videos

Last Updated: Aug 30, 2025

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
Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
05:17

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

Published on: July 28, 2016

10.4K
Stimulation of Stem Cell Niches and Tissue Regeneration in Mouse Skin by Switchable Protoporphyrin IX-Dependent Photogeneration of Reactive Oxygen Species In Situ
10:05

Stimulation of Stem Cell Niches and Tissue Regeneration in Mouse Skin by Switchable Protoporphyrin IX-Dependent Photogeneration of Reactive Oxygen Species In Situ

Published on: May 8, 2020

2.0K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Heme (protoheme IX) is a vital cofactor for numerous proteins involved in electron transfer and gas binding.
  • Most organisms capable of utilizing heme synthesize it endogenously, rather than obtaining it from diet.
  • Dietary heme is primarily used as an iron source, not for heme synthesis.

Purpose of the Study:

  • To review the three known pathways for heme biosynthesis.
  • To discuss the two known pathways for 5-aminolevulinate (ALA) synthesis.
  • To explore unique characteristics of heme biosynthesis enzymes, regulation, and associated disorders.

Main Methods:

  • Comparative analysis of heme biosynthesis pathways.
  • Review of enzymatic mechanisms in heme synthesis.
  • Examination of regulatory mechanisms and genetic disorders related to heme production.

Main Results:

  • Identified three distinct heme biosynthesis pathways: siroheme-dependent (SHD), coproporphyrin-dependent (CPD), and protoporphyrin-dependent (PPD).
  • All pathways share common enzymes converting 5-aminolevulinate (ALA) to uroporphyrinogen III.
  • Detailed the two known pathways for ALA synthesis.

Conclusions:

  • Heme biosynthesis is conserved across life, with variations in specific pathways (SHD, CPD, PPD) across different organisms.
  • Understanding these pathways is crucial for comprehending cellular functions and metabolic disorders.
  • Further research into enzyme function and regulation can illuminate therapeutic targets for heme-related diseases.