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

Preparation of Amines: Reduction of Oximes and Nitro Compounds01:29

Preparation of Amines: Reduction of Oximes and Nitro Compounds

Oximes can be reduced to primary amines using catalytic hydrogenation, hydride reduction, or sodium metal reduction. The reduction of aliphatic and aromatic nitro compounds to primary amines takes place by either catalytic hydrogenation or by using active metals like Fe, Zn, and Sn in the presence of an acid.
Though catalytic hydrogenation can reduce nitrobenzenes, the reduction is nonselective in the presence of other functional groups. For instance, if nitrobenzene contains an aldehyde group,...
Phase I Reactions: Reductive Reactions01:27

Phase I Reactions: Reductive Reactions

Phase I biotransformation reductive reactions are chemical processes that modify drugs by introducing or revealing polar functional groups via reduction. Enzymes called reductases catalyze these reactions, playing a pivotal role in drug metabolism by transforming lipophilic drugs into more polar, water-soluble metabolites for easy excretion. An essential type of reductive reaction is the carbonyl group reduction, where aldehydes and ketones are reduced to alcohols. An example is the...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

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...
Inorganic Nitrogen Assimilation01:22

Inorganic Nitrogen Assimilation

Nitrogen is an essential element in biological systems, forming a crucial component of proteins, nucleic acids, and other cellular constituents. Many bacteria and archaea acquire nitrogen in the form of nitrate (NO₃⁻) or ammonia (NH₃), which are then assimilated into biomolecules through specific enzymatic pathways.Assimilatory Nitrate ReductionWhen nitrate enters the cell, it undergoes a two-step reduction process known as assimilatory nitrate reduction. Initially, the enzyme nitrate reductase...
2° Amines to N-Nitrosamines: Reaction with NaNO201:20

2° Amines to N-Nitrosamines: Reaction with NaNO2

Secondary amines react with nitrous acid to form N-nitrosamines, as depicted in Figure 1. Nitrous acid, a weak and unstable acid, is formed in situ from an aqueous solution of sodium nitrite and strong acids, such as hydrochloric acid or sulfuric acid, in cold conditions. In the presence of an acid, the nitrous acid gets protonated. The subsequent loss of water results in the formation of the electrophile known as nitrosonium ion.
Resonance02:52

Resonance

The Lewis structure of a nitrite anion (NO2−) may actually be drawn in two different ways, distinguished by the locations of the N-O and N=O bonds.

You might also read

Related Articles

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

Sort by
Same author

Stabilization of Transaminases in Aqueous-Organic Media by Pyridoxal-5'-phosphate: A Case Study of Transaminase from Desulfomonile tiedjei.

Acta naturae·2026
Same author

Insights into the Functioning of the D-amino Acid Transaminase from Haliscomenobacter Hydrossis via a Structural and Spectral Analysis of its Complex with 3-Aminooxypropionic Acid.

Acta naturae·2024
Same author

Single-point substitution F97M leads to in cellulo crystallization of the biphotochromic protein moxSAASoti.

Biochemical and biophysical research communications·2024
Same author

PDSTP Is the First Drug in Class to Treat Coronavirus Infection.

Herald of the Russian Academy of Sciences·2022
Same author

[Comprehensive medical rehabilitation using therapeutic physical factors including hydrokinesiotherapy in a pool with mineral water and its effect on circadian rhythms of arterial pressure and autonomic regulation in patients with arterial hypertension and with chronic psychoemotional stress].

Voprosy kurortologii, fizioterapii, i lechebnoi fizicheskoi kultury·2022
Same author

Highly-Active Recombinant Formate Dehydrogenase from Pathogenic Bacterium Staphylococcus aureus: Preparation and Crystallization.

Biochemistry. Biokhimiia·2020

Related Experiment Video

Updated: May 16, 2026

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

Octaheme nitrite reductases: structure and properties.

T V Tikhonova1, A A Trofimov, V O Popov

  • 1Bach Institute of Biochemistry, Russian Academy of Sciences, 119071 Moscow, Russia. ttikhonova@inbi.ras.ru

Biochemistry. Biokhimiia
|November 20, 2012
PubMed
Summary
This summary is machine-generated.

Octaheme nitrite reductases bridge the evolution of nitrogen cycle enzymes, uniquely combining features of older reductases and newer oxidases. These transitional enzymes play a key role in bacterial nitrogen cycling.

More Related Videos

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

Related Experiment Videos

Last Updated: May 16, 2026

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

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

Area of Science:

  • Biochemistry
  • Microbiology
  • Environmental Science

Background:

  • Octaheme oxidoreductases are crucial bacterial enzymes in the nitrogen cycle.
  • Their evolution from pentaheme nitrite reductases involved a functional shift from nitrogen oxide reduction to oxidation.
  • Octaheme nitrite reductases represent a transitional form with unique characteristics.

Purpose of the Study:

  • To review structure-function investigations of octaheme nitrite reductases.
  • To compare octaheme nitrite reductases with other multiheme nitrogen cycle oxidoreductases.

Main Methods:

  • Literature review focusing on structure-function data.
  • Comparative analysis of enzyme families.

Main Results:

  • Octaheme nitrite reductases exhibit a unique blend of ancestral and derived enzymatic features.
  • These enzymes possess distinct structural and functional properties compared to related oxidoreductases.
  • Their transitional nature highlights evolutionary adaptations in the nitrogen cycle.

Conclusions:

  • Octaheme nitrite reductases are key transitional enzymes in the bacterial nitrogen cycle.
  • Understanding their structure-function relationships provides insights into enzyme evolution.
  • These enzymes are vital for comprehending the biogeochemical cycling of nitrogen.