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

6.7K
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...
6.7K
ATP Synthase: Structure01:18

ATP Synthase: Structure

16.2K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
16.2K
Electron Transport Chains01:28

Electron Transport Chains

85.6K
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...
85.6K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

11.9K
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...
11.9K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.0K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
16.0K
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

8.4K
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...
8.4K

You might also read

Related Articles

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

Sort by
Same author

Development of High-Affinity CHD1 Chromodomain Inhibitors.

Journal of medicinal chemistry·2026
Same author

Stabilizing Plasmodium falciparum proteins for small molecule drug discovery.

Protein science : a publication of the Protein Society·2026
Same author

Trafficking of a nitrogenase FeMo-cofactor assembly intermediate.

Nature chemical biology·2026
Same author

From Pharmacophore to Warhead: NAD<sup>+</sup>-Targeting Triazoles as Mechanism-Based Sirtuin Inhibitors.

Angewandte Chemie (International ed. in English)·2025
Same author

Structural evolution of nitrogenase over 3 billion years.

eLife·2025
Same author

<i>Escherichia coli</i> Triheme Enzyme YhjA: Structure and Reactivity.

Biochemistry·2025
Same journal

Iron-ascorbate complex formation and redox behavior in Tris buffer under aerobic and anaerobic conditions: relevance to iron-deficiency anemia.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026
Same journal

The development of bioinspired copper complexes for CO<sub>2</sub> activation and hydration.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026
Same journal

Retraction Note: Surface modification minimizes the toxicity of silver nanoparticles: an in vitro and in vivo study.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026
Same journal

A meeting of minds, mechanisms and memories - editorial to JBIC Special Issue on Bio-electrochemistry in honor of Fraser Armstrong.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026
Same journal

Correction: The evolutionary footprint of histidine in hemoglobin and myoglobin: an implication towards their function.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026
Same journal

Pharmacokinetics and Efficacy of a Cyanide-Neutralizing [Mo<sub>2</sub>O<sub>2</sub>(µ-S)<sub>2</sub>]<sup>2+</sup> Based Metallodrug in NMRI Mice.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026
See all related articles

Related Experiment Video

Updated: May 2, 2026

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

9.3K

Nitrogenase FeMo cofactor: an atomic structure in three simple steps.

Oliver Einsle1

  • 1BIOSS Centre for Biological Signalling Studies, Schänzlestr. 1, 79104, Freiburg, Germany, einsle@biochemie.uni-freiburg.de.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|February 22, 2014
PubMed
Summary
This summary is machine-generated.

The FeMo cofactor in nitrogenase, essential for converting nitrogen to ammonia, has a complex atomic structure. Decades of research and X-ray crystallography revealed its unique nature, though its catalytic mechanism still requires further investigation.

More Related Videos

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction
10:57

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction

Published on: April 10, 2018

17.5K
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

12.7K

Related Experiment Videos

Last Updated: May 2, 2026

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

9.3K
Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction
10:57

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction

Published on: April 10, 2018

17.5K
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

12.7K

Area of Science:

  • Bioinorganic Chemistry
  • Enzymology
  • Structural Biology

Background:

  • Nitrogenase is crucial for biological nitrogen fixation, converting dinitrogen to ammonia.
  • The molybdenum-iron (MoFe) cofactor is the catalytic center of nitrogenase.
  • Understanding the FeMo cofactor's structure is key to elucidating nitrogenase's mechanism.

Purpose of the Study:

  • To review the protracted history of FeMo cofactor structure determination.
  • To highlight the challenges and unexpected findings during structural elucidation.
  • To discuss the current understanding of the FeMo cofactor's atomic structure.

Main Methods:

  • X-ray crystallography over two decades.
  • Iterative refinement and correction of structural models.
  • Analysis of the unique [Mo:7Fe:9S:C]:homocitrate cluster.

Main Results:

  • The atomic structure of the FeMo cofactor has been definitively determined.
  • The FeMo cofactor is the largest known iron-sulfur cluster in bioinorganic chemistry.
  • Its unique composition and structure presented significant challenges to researchers.

Conclusions:

  • The complete atomic structure of the FeMo cofactor is now established.
  • Despite structural resolution, the catalytic mechanism of nitrogenase remains incompletely understood.
  • Further research is needed to fully explain the enzyme's function.