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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K
Improving Translational Accuracy02:07

Improving Translational Accuracy

11.7K
Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
11.7K
Metal-Ligand Bonds02:51

Metal-Ligand Bonds

21.1K
The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
21.1K
tRNA Activation02:26

tRNA Activation

19.4K
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
19.4K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

5.8K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.8K
EDTA: Auxiliary Complexing Reagents01:26

EDTA: Auxiliary Complexing Reagents

631
EDTA titrations are usually carried out in highly basic conditions, where the fully deprotonated form of EDTA, Y4−, actively complexes with the free metal ions in the solution. Several metal ions precipitate as hydrous oxide (hydroxides, oxides, or oxyhydroxides) under these conditions, lowering the concentration of free metal ions in the solution. For this reason, auxiliary complexing agents or ligands such as ammonia, tartrate, citrate, or triethanolamine are used in EDTA titrations to...
631

You might also read

Related Articles

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

Sort by
Same author

Switchable reactivity of homopropargylic alcohols towards γ-arylated ketones and α-arylated tetrahydrofurans in HFIP.

Chemical science·2026
Same author

Electrochemical <i>N</i>‑Propargylation of <i>N</i>‑Heterocycles via Decarboxylation of Allenoic Acids.

ACS organic & inorganic Au·2026
Same author

Progress toward a Nonenzymatic Gluconeogenesis: One-Pot Reactions and Model Systems.

JACS Au·2026
Same author

A Nonenzymatic Analogue of the Biosynthesis of Pyridoxal Vitamers.

Journal of the American Chemical Society·2026
Same author

Shadow metabolism at interfaces.

Nature chemical biology·2026
Same author

Hexafluoroisopropanol-Mediated Cascade Cyclization for Construction of α‑Amino-γ-spirolactones.

JACS Au·2025

Related Experiment Video

Updated: Jul 27, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.6K

Metal-Pyridoxal Cooperativity in Nonenzymatic Transamination.

Quentin Dherbassy1, Robert J Mayer1, Kamila B Muchowska1

  • 1Université de Strasbourg, CNRS, ISIS & icFRC, 8 Allée Gaspard Monge, 67000 Strasbourg, France.

Journal of the American Chemical Society
|June 6, 2023
PubMed
Summary

Metal ions like iron and aluminum significantly boost the catalytic activity of pyridoxal (PL), a coenzyme, in transamination reactions. This suggests coenzymes could have functioned catalytically before the evolution of enzymes, offering insights into early life chemistry.

More Related Videos

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.3K

Related Experiment Videos

Last Updated: Jul 27, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.6K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.3K

Area of Science:

  • Origin of Life Studies
  • Biochemistry
  • Catalysis

Background:

  • Coenzymes are crucial in over 30% of enzymatic reactions and may predate enzymes.
  • The catalytic potential of coenzymes as organocatalysts, especially in prebiotic chemistry, remains poorly understood.
  • Metal ions are known catalysts for metabolic reactions, even without enzymes.

Purpose of the Study:

  • To investigate the influence of metal ions on coenzyme catalysis under conditions relevant to the origin of life.
  • To explore the synergistic effects of abundant metal ions (Fe, Al) with pyridoxal (PL) in transamination reactions.

Main Methods:

  • Studied transamination reactions catalyzed by pyridoxal (PL) and pyridoxal phosphate (PLP) in the presence of Fe3+ and Al3+ ions.
  • Conducted experiments under conditions mimicking the early Earth (20-75 °C, pH 5-7.5).
  • Employed experimental and theoretical mechanistic studies to elucidate reaction pathways.

Main Results:

  • Fe3+-PL and Al3+-PL complexes showed significantly enhanced transamination catalysis compared to PL or metal ions alone.
  • Al3+-PL catalysis was over 1000 times faster than PL alone under milder conditions.
  • Metal coordination to PL altered the reaction mechanism and slowed imine intermediate hydrolysis.

Conclusions:

  • Pyridoxal derivatives, in conjunction with metal ions, could have possessed significant catalytic activity predating enzyme evolution.
  • This finding provides a plausible mechanism for early biochemical reactions in prebiotic environments.
  • Coenzymes may have played a crucial catalytic role in the emergence of life.