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

Lipid Catabolism01:25

Lipid Catabolism

627
Triglycerides serve as crucial long-term energy storage molecules in microorganisms, providing a dense source of metabolic energy. Their breakdown is mediated by lipases, which hydrolyze triglycerides into glycerol and free fatty acids. Each of these components follows distinct metabolic pathways, ultimately contributing to ATP synthesis and cellular energy homeostasis.Glycerol MetabolismGlycerol, released from triglyceride hydrolysis, is phosphorylated by glycerol kinase to form...
627
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.8K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.8K
Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

3.7K
Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...
3.7K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

17.7K
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...
17.7K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.8K
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...
8.8K
Carbon-dioxide Fixation01:28

Carbon-dioxide Fixation

467
Carbon dioxide fixation in prokaryotes enables the assimilation of inorganic carbon into organic molecules, supporting biosynthetic pathways, sustaining ecosystems, and contributing to the global carbon cycle. It also has industrial applications in carbon capture and bioproduct synthesis. Autotrophic organisms rely on this process to utilize CO₂ as a carbon source in diverse environments.The Calvin CycleThe Calvin cycle is the most widespread carbon fixation mechanism, primarily used by...
467

You might also read

Related Articles

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

Sort by
Same author

The Mycobacterium tuberculosis Rv0132c Gene Product Mtb-FGD2 Can Act as an F<sub>420</sub>-Dependent Glucose Dehydrogenase.

Proteins·2026
Same author

Integrated structural dynamics uncover a new B<sub>12</sub> photoreceptor activation mode.

Nature·2026
Same author

Structure and Mechanism of PhdC, a Prenylated-Flavin Maturase.

Proteins·2025
Same author

Fragment-Based Development of Small Molecule Inhibitors Targeting <i>Mycobacterium tuberculosis</i> Cholesterol Metabolism.

Journal of medicinal chemistry·2025
Same author

Engineered enzymes for enantioselective nucleophilic aromatic substitutions.

Nature·2025
Same author

Fragment-based development of small molecule inhibitors targeting <i>Mycobacterium tuberculosis</i> cholesterol metabolism.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Dec 10, 2025

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

767

Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope.

Tom Halliwell1, Karl Fisher1, Karl A P Payne1,2

  • 1Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.

Microorganisms
|September 5, 2020
PubMed
Summary
This summary is machine-generated.

Reductive dehalogenases cleave carbon-halogen bonds. This study reveals the crystal structure of a specific enzyme, NpRdhA, showing a direct cobalt-halogen interaction and enabling protein engineering for bioremediation applications.

Keywords:
EPRX-ray crystallographybioremediationcobalaminiron-sulphur clustersreductive dehalogenase

More Related Videos

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
20:28

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments

Published on: October 2, 2012

14.4K
Development of Sulfidogenic Sludge from Marine Sediments and Trichloroethylene Reduction in an Upflow Anaerobic Sludge Blanket Reactor
15:19

Development of Sulfidogenic Sludge from Marine Sediments and Trichloroethylene Reduction in an Upflow Anaerobic Sludge Blanket Reactor

Published on: October 15, 2015

10.0K

Related Experiment Videos

Last Updated: Dec 10, 2025

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

767
A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
20:28

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments

Published on: October 2, 2012

14.4K
Development of Sulfidogenic Sludge from Marine Sediments and Trichloroethylene Reduction in an Upflow Anaerobic Sludge Blanket Reactor
15:19

Development of Sulfidogenic Sludge from Marine Sediments and Trichloroethylene Reduction in an Upflow Anaerobic Sludge Blanket Reactor

Published on: October 15, 2015

10.0K

Area of Science:

  • Biochemistry
  • Enzymology
  • Environmental Microbiology

Background:

  • Reductive dehalogenases catalyze the cleavage of carbon-halogen bonds, crucial for organohalide respiration.
  • Mechanisms proposed include organocobalt, radical, or cobalt-halide adduct catalysis.
  • The oxygen-tolerant Nitratireductor pacificus pht-3B catabolic reductive dehalogenase (NpRdhA) was investigated.

Purpose of the Study:

  • To elucidate the catalytic mechanism of NpRdhA.
  • To determine the structural basis for substrate preference in NpRdhA.
  • To explore protein engineering strategies for modifying NpRdhA's substrate specificity.

Main Methods:

  • X-ray crystallography of substrate-bound NpRdhA.
  • Observation of in crystallo product formation via X-ray photoreduction.
  • Protein engineering techniques.

Main Results:

  • First crystal structures of substrate-bound NpRdhA were obtained.
  • A direct cobalt-halogen interaction was confirmed, explaining substrate preference.
  • X-ray photoreduction led to observed product formation within crystals.

Conclusions:

  • The crystal structures provide a detailed understanding of NpRdhA's catalytic mechanism.
  • Protein engineering successfully altered NpRdhA's substrate preference.
  • These findings offer a blueprint for utilizing NpRdhA and related enzymes in bioremediation.