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

Cofactors and Coenzymes01:24

Cofactors and Coenzymes

12.4K
Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
12.4K
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

86.1K
Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
86.1K
Minerals01:26

Minerals

849
Minerals are essential nutrients that the human body needs in small amounts to work properly. They play a vital role in many bodily functions, such as building strong bones and transmitting nerve impulses. Some minerals are needed for hormone production or to maintain a normal heartbeat. Major minerals include calcium, phosphorus, potassium, sulfur, sodium, chlorine, and magnesium, while trace minerals include iron, manganese, copper, iodine, zinc, cobalt, fluoride, and selenium.
 
Major...
849
Sulfur Assimilation01:20

Sulfur Assimilation

220
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
220
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

15.5K
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...
15.5K
Inborn Errors of Metabolism01:20

Inborn Errors of Metabolism

601
Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...
601

You might also read

Related Articles

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

Sort by
Same author

Lysophosphatidylcholine as a mechanistic and therapeutic nexus in atherosclerotic cardiovascular disease.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2026
Same author

Sulfite oxidase deficiency causes persulfidation loss and hydrogen sulfide release.

The Journal of clinical investigation·2025
Same author

Gephyrin filaments represent the molecular basis of inhibitory postsynaptic densities.

Nature communications·2025
Same author

Phosphoinositide- and Collybistin-Dependent Synaptic Clustering of Gephyrin.

Journal of neurochemistry·2025
Same author

A prevalent MOCS2 variant in the Roma population is associated with a novel mild form of molybdenum cofactor deficiency.

European journal of pediatrics·2025
Same author

Increased Survival in Patients With Molybdenum Cofactor Deficiency Type A Treated With Cyclic Pyranopterin Monophosphate.

Journal of inherited metabolic disease·2025

Related Experiment Video

Updated: Dec 6, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K

Molybdenum cofactor biology, evolution and deficiency.

Simon J Mayr1, Ralf-R Mendel2, Guenter Schwarz1

  • 1Institute of Biochemistry, Department of Chemistry, Center for Molecular Medicine, University of Cologne, Zuelpicher Str. 47, 50674 Koeln, Germany.

Biochimica Et Biophysica Acta. Molecular Cell Research
|October 5, 2020
PubMed
Summary
This summary is machine-generated.

The ancient molybdenum cofactor (Moco) is crucial for life

Keywords:
Alternative splicingCysteine catabolismInhibitory synapseIron‑sulfur clusterMitochondriaMolybdenum cofactor

More Related Videos

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase COX/SDH Double-labeling Histochemistry
06:53

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase COX/SDH Double-labeling Histochemistry

Published on: November 23, 2011

37.4K
Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples
04:32

Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples

Published on: October 14, 2021

3.0K

Related Experiment Videos

Last Updated: Dec 6, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K
Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase COX/SDH Double-labeling Histochemistry
06:53

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase COX/SDH Double-labeling Histochemistry

Published on: November 23, 2011

37.4K
Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples
04:32

Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples

Published on: October 14, 2021

3.0K

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Genetics

Background:

  • The molybdenum cofactor (Moco) is an ancient metallo-sulfur cofactor essential for numerous biological processes.
  • Moco biosynthesis genes trace back to the last universal common ancestor (LUCA) and have evolved significantly.
  • Gene fusions in Moco biosynthesis have provided evolutionary advantages and led to new functions.

Purpose of the Study:

  • To review the evolutionary benefits of gene fusions in eukaryotic Moco biosynthesis.
  • To explore how gene fusions contributed to both biosynthetic efficiency and the development of novel functions.
  • To highlight the diverse cellular roles of Moco biosynthetic genes and associated disorders.

Main Methods:

  • Literature review of Moco biosynthesis and evolution in eukaryotes.
  • Analysis of gene fusion events and their impact on Moco pathway efficiency.
  • Examination of the link between Moco gene products and cellular functions/disorders.

Main Results:

  • Gene fusions in Moco biosynthesis enhance coordinated expression and substrate channeling.
  • These fusions have been a source of evolutionary innovation, leading to new protein functions.
  • Moco biosynthetic genes are implicated in various cellular processes, and their dysfunction causes severe disorders.

Conclusions:

  • Gene fusions have played a critical role in the evolution and optimization of Moco biosynthesis in eukaryotes.
  • The dual role of Moco genes in biosynthesis and other cellular functions underscores their importance.
  • Understanding Moco gene evolution is vital for comprehending metabolic pathways and associated human diseases.