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

ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

15.3K
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...
15.3K
Aldehydes and Ketones with HCN: Cyanohydrin Formation Mechanism01:10

Aldehydes and Ketones with HCN: Cyanohydrin Formation Mechanism

3.4K
Cyanohydrins are formed when cyanide nucleophiles and carbonyl compounds like aldehydes and ketones react. A strong base, the cyanide ion, catalyzes cyanohydrin formation. The ions are generated from HCN under aqueous conditions. Once the cyanide ions are generated, the first step involves the nucleophilic attack of the cyanide ions on the electrophilic carbonyl carbon. This attack shifts the π electrons from the C=O to the oxygen atom forming the alkoxide ion intermediate. The alkoxide anion...
3.4K
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

6.7K
Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
6.7K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.2K
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...
8.2K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

15.1K
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...
15.1K
ATP Synthase: Structure01:18

ATP Synthase: Structure

13.2K
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...
13.2K

You might also read

Related Articles

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

Sort by
Same author

Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism.

Acta crystallographica. Section D, Structural biology·2017
Same author

Concerted action of two subunits of the functional dimer of Shewanella oneidensis MR-1 uridine phosphorylase derived from a comparison of the C212S mutant and the wild-type enzyme.

Acta crystallographica. Section D, Structural biology·2016
Same author

Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada.

Acta crystallographica. Section F, Structural biology communications·2015
Same author

Structural study of the X-ray-induced enzymatic reaction of octahaem cytochrome C nitrite reductase.

Acta crystallographica. Section D, Biological crystallography·2015
Same author

Physicochemical characterization of uridine phosphorylase from Shewanella oneidensis MR-1.

Doklady. Biochemistry and biophysics·2013
Same author

Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutant.

Acta crystallographica. Section D, Biological crystallography·2013

Related Experiment Video

Updated: Sep 18, 2025

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

10.2K

[Mechanism of Thiocyanate Dehydrogenase Functioning Based on Structural Data].

K M Polyakov1,2, S Gavryushov1

  • 1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia.

Molekuliarnaia Biologiia
|June 21, 2025
PubMed
Summary

New high-resolution structures reveal thiocyanate dehydrogenase

Keywords:
X-ray analysis of proteinsconformational changesenzymatic reactionsmulticopper enzymes

More Related Videos

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
05:57

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

499
Preparation of SNS CobaltII Pincer Model Complexes of Liver Alcohol Dehydrogenase
06:31

Preparation of SNS CobaltII Pincer Model Complexes of Liver Alcohol Dehydrogenase

Published on: March 19, 2020

7.2K

Related Experiment Videos

Last Updated: Sep 18, 2025

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

10.2K
Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
05:57

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

499
Preparation of SNS CobaltII Pincer Model Complexes of Liver Alcohol Dehydrogenase
06:31

Preparation of SNS CobaltII Pincer Model Complexes of Liver Alcohol Dehydrogenase

Published on: March 19, 2020

7.2K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Context:

  • Thiocyanate dehydrogenase (TCDH) catalyzes the oxidation of thiocyanate to cyanate.
  • Previous TCDH structures from Thioalkalivibrio paradoxus had limitations in resolution and data completeness.
  • Understanding TCDH mechanism is crucial for bioinorganic chemistry and environmental science.

Purpose:

  • To elucidate the high-resolution structure of a gene-modified thiocyanate dehydrogenase from Ptlomicrobium methylotrophicum.
  • To investigate the enzyme's active site, copper ion states, and substrate/inhibitor binding.
  • To propose a refined mechanism for thiocyanate oxidation based on new structural data.

Summary:

  • High-resolution structures of Ptlomicrobium methylotrophicum TCDH reveal two distinct conformations (open and closed active sites) with fully occupied copper ions.
  • Superposition of different copper ion oxidation states and ligand coordination within each conformation provides detailed insights.
  • Complexes with thiourea and oxygen in the closed conformation facilitate modeling of substrate binding and oxygen activation.

Impact:

  • Provides unprecedented atomic-level detail of thiocyanate dehydrogenase structure and function.
  • Enables a more accurate understanding of the enzymatic reaction mechanism, including oxygen activation.
  • Advances knowledge in bioinorganic chemistry and the catalytic roles of copper enzymes.