Jove
Visualize
Contact Us

Related Concept Videos

Fixing Double-strand Breaks02:04

Fixing Double-strand Breaks

14.6K
The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...
14.6K
Fixing Double-strand Breaks02:04

Fixing Double-strand Breaks

4.4K
4.4K
Conjugated Proteins02:50

Conjugated Proteins

28.6K
Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
28.6K
Protein Families02:47

Protein Families

16.8K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
16.8K
Activation Energy01:26

Activation Energy

86.6K
Activation energy is the minimum amount of energy necessary for a chemical reaction to move forward. The higher the activation energy, the slower the rate of the reaction. However, adding heat to the reaction will increase the rate, since it causes molecules to move faster and increase the likelihood that molecules will collide. The collision and breaking of bonds represents the uphill phase of a reaction and generates the transition state. The transition state is an unstable high-energy state...
86.6K
Protein Digestion01:02

Protein Digestion

110.9K
Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
110.9K

You might also read

Related Articles

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

Sort by
Same author

Biochemical and functional characterization of <i>Porphyromonas gingivalis</i> HmuS protein reveals its participation in heme metabolism.

Frontiers in microbiology·2026
Same author

Commensal gut bacteria employ de-chelatase HmuS to harvest iron from heme.

The EMBO journal·2025
Same author

Epic science.

Trends in biochemical sciences·2025
Same author

Long-Range Allosteric Communication Modulated by Active Site Mn(II) Coordination Drives Catalysis in <i>Xanthobacter autotrophicus</i> Acetone Carboxylase.

International journal of molecular sciences·2025
Same author

Upcycling lignin with a controlled burn.

Trends in biochemical sciences·2025
Same author

Heme and iron limitation in a GI-tract foundation species leads to a reshuffling of the metalloproteome and a shift toward manganese usage.

Frontiers in chemistry·2025
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 Experiment Video

Updated: Jan 28, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

12.5K

Making and breaking heme.

Arianna I Celis1, Jennifer L DuBois1

  • 1Montana State University, 103 Chemistry and Biochemistry, Bozeman, MT 59717, United States.

Current Opinion in Structural Biology
|February 26, 2019
PubMed
Summary
This summary is machine-generated.

Heme cofactor synthesis and breakdown pathways are surprisingly diverse across organisms. This diversity reflects varied oxygen use and membrane structures, offering new antimicrobial targets.

More Related Videos

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
05:08

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Published on: January 31, 2022

5.6K
Bioluminescence Imaging of Heme Oxygenase-1 Upregulation in the Gua Sha Procedure
06:39

Bioluminescence Imaging of Heme Oxygenase-1 Upregulation in the Gua Sha Procedure

Published on: August 28, 2009

14.4K

Related Experiment Videos

Last Updated: Jan 28, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

12.5K
Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
05:08

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Published on: January 31, 2022

5.6K
Bioluminescence Imaging of Heme Oxygenase-1 Upregulation in the Gua Sha Procedure
06:39

Bioluminescence Imaging of Heme Oxygenase-1 Upregulation in the Gua Sha Procedure

Published on: August 28, 2009

14.4K

Area of Science:

  • Biochemistry
  • Microbiology
  • Evolutionary Biology

Background:

  • The heme b cofactor (heme) is essential for numerous biological processes.
  • Heme metabolism pathways were previously thought to be conserved.

Purpose of the Study:

  • To explore the diversity of heme biosynthesis and degradation pathways.
  • To understand the evolutionary divergence of these pathways in different organisms.
  • To identify potential targets for antimicrobial development and ecological monitoring.

Main Methods:

  • Comparative analysis of heme metabolic enzymes across diverse taxa.
  • Investigation of pathway variations related to oxygen utilization and cellular organization.

Main Results:

  • Heme biosynthesis pathways have diverged at least twice evolutionarily.
  • At least three distinct families of heme degradases have been identified.
  • Pathway variations correlate with organismal oxygen dependency and membrane structure.

Conclusions:

  • Heme metabolism exhibits greater diversity than previously recognized.
  • Understanding heme pathway divergence is crucial for developing novel antimicrobials.
  • Heme turnover mechanisms provide insights into organismal and ecological functions.