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

Oxymercuration-Reduction of Alkenes02:36

Oxymercuration-Reduction of Alkenes

8.1K
Oxymercuration–reduction of alkenes is one of the major reactions converting alkenes to alcohols. It involves the hydration of alkenes with mercuric acetate in a mixture of tetrahydrofuran and water, forming an organomercury adduct. This is followed by a demercuration step in which the adduct is reduced to an alcohol using sodium borohydride.
8.1K
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide02:44

Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

10.9K
Alkenes are converted to 1,2-diols or glycols through a process called dihydroxylation. It involves the addition of two hydroxyl groups across the double bond with two different stereochemical approaches, namely anti and syn. Dihydroxylation using osmium tetroxide progresses with syn stereochemistry.
10.9K
Hydroboration-Oxidation of Alkenes03:08

Hydroboration-Oxidation of Alkenes

9.9K
In addition to the oxymercuration–demercuration method, which converts the alkenes to alcohols with Markovnikov orientation, a complementary hydroboration-oxidation method yields the anti-Markovnikov product. The hydroboration reaction, discovered in 1959 by H.C. Brown, involves the addition of a B–H bond of borane to an alkene giving an organoborane intermediate. The oxidation of this intermediate with basic hydrogen peroxide forms an alcohol.
9.9K
Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids02:04

Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids

6.0K
Diols are compounds with two hydroxyl groups. In addition to syn dihydroxylation, diols can also be synthesized through the process of anti dihydroxylation. The process involves treating an alkene with a peroxycarboxylic acid to form an epoxide. Epoxides are highly strained three-membered rings with oxygen and two carbons occupying the corners of an equilateral triangle. This step is followed by ring-opening of the epoxide in the presence of an aqueous acid to give a trans diol.
6.0K
Electrophilic Addition of HX to 1,3-Butadiene: Thermodynamic vs Kinetic Control01:23

Electrophilic Addition of HX to 1,3-Butadiene: Thermodynamic vs Kinetic Control

3.4K
The addition of a hydrogen halide to 1,3-butadiene gives a mixture of 1,2- and 1,4-adducts. Since more substituted alkenes are more stable, the 1,4-adduct is expected to be the major product. However, the product distribution is strongly influenced by temperature; low temperature favors the 1,2-adduct, whereas the 1,4-adduct is predominant at high temperature.
3.4K
Regioselectivity and Stereochemistry of Hydroboration02:36

Regioselectivity and Stereochemistry of Hydroboration

7.7K
A significant aspect of hydroboration–oxidation is the regio- and stereochemical outcome of the reaction.
Hydroboration proceeds in a concerted fashion with the attack of borane on the π bond, giving a cyclic four-centered transition state. The –BH2 group is bonded to the less substituted carbon and –H to the more substituted carbon. The concerted nature requires the simultaneous addition of –H and –BH2 across the same face of the alkene giving syn...
7.7K

You might also read

Related Articles

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

Sort by
Same author

Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.

Journal of molecular biology·2026
Same author

Magnesium as a conformational gatekeeper of KRAS: Structural dynamics and therapeutic implications.

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

Magnesium as a Conformational Gatekeeper of KRAS: Structural Dynamics and Therapeutic Implications.

bioRxiv : the preprint server for biology·2026
Same author

Correction: Dynamic conformational equilibria in the active states of KRAS and NRAS.

RSC chemical biology·2026
Same author

A druggable redox switch on SHP1 controls macrophage inflammation.

Nature chemical biology·2026
Same author

A druggable redox switch on SHP1 controls macrophage inflammation.

bioRxiv : the preprint server for biology·2026
Same journal

Switching Site Selectivity in Alkoxyamine Hydration: From Lone-Pair Direction to Solvent Network Dominance.

Journal of the American Chemical Society·2026
Same journal

A Topotactic Leap: 2D Layers to 3D Large-Pore Zeolite.

Journal of the American Chemical Society·2026
Same journal

Enhanced Hydrogen Evolution over Single-Atom Catalysts via Electrostatic Polarization in Contact-electro-catalysis.

Journal of the American Chemical Society·2026
Same journal

Tumor Acidity-Activatable Ionizable Lipid Nanoparticles for Selective Oncolytic Therapy.

Journal of the American Chemical Society·2026
Same journal

Alternating Magnetic Field Promotes Ammonia Cracking by Disrupting the Sabatier Limitation of Ruthenium Catalytic Species.

Journal of the American Chemical Society·2026
Same journal

Bulk Ferromagnetic Icosahedral Quasicrystals without Rapid Quenching.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: Apr 28, 2026

Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase
10:33

Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase

Published on: October 15, 2018

7.3K

Electron transfer control in soluble methane monooxygenase.

Weixue Wang1, Roxana E Iacob, Rebecca P Luoh

  • 1Departments of †Chemistry and §Biological Engineering, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.

Journal of the American Chemical Society
|June 18, 2014
PubMed
Summary
This summary is machine-generated.

Bacterial multicomponent monooxygenases (BMMs) use multiple proteins for hydrocarbon oxidation. We found that regulatory proteins inhibit reductase binding, controlling electron transfer to the enzyme's active site.

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

17.6K
Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies
05:30

Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies

Published on: January 23, 2019

15.6K

Related Experiment Videos

Last Updated: Apr 28, 2026

Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase
10:33

Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase

Published on: October 15, 2018

7.3K
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

17.6K
Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies
05:30

Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies

Published on: January 23, 2019

15.6K

Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial metabolism

Background:

  • Bacterial multicomponent monooxygenases (BMMs) catalyze hydrocarbon hydroxylation/epoxidation via multi-protein complexes.
  • The precise interactions between BMM components and the roles of regulatory proteins in electron transfer remain unclear.

Purpose of the Study:

  • To elucidate the reductase binding site on the hydroxylase component of soluble methane monooxygenase (sMMO).
  • To investigate the role of regulatory proteins in modulating intermolecular electron transfer in sMMO.

Main Methods:

  • X-ray crystallography or cryo-EM to determine protein structures.
  • Biochemical assays to measure electron transfer rates.
  • Mutagenesis studies to probe protein-protein interactions.

Main Results:

  • The ferredoxin domain of the reductase binds to the hydroxylase's canyon region.
  • This canyon region is also the binding site for regulatory proteins.
  • Regulatory proteins inhibit reductase binding, thereby controlling electron transfer.

Conclusions:

  • A competitive binding mechanism between regulatory proteins and reductases regulates electron transfer in sMMO.
  • This mechanism likely extends to other bacterial multicomponent monooxygenases.