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

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

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...
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide02:44

Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

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.
Oxidative Cleavage of Alkenes: Ozonolysis01:46

Oxidative Cleavage of Alkenes: Ozonolysis

In ozonolysis, ozone is used to cleave a carbon–carbon double bond to form aldehydes and ketones, or carboxylic acids, depending on the work-up.
Ozone is a symmetrical bent molecule stabilized by a resonance structure.
Oxidation of Alkenes: Syn Dihydroxylation with Potassium Permanganate02:21

Oxidation of Alkenes: Syn Dihydroxylation with Potassium Permanganate

Alkenes can be dihydroxylated using potassium permanganate. The method encompasses the reaction of an alkene with a cold, dilute solution of potassium permanganate under basic conditions to form a cis-diol along with a brown precipitate of manganese dioxide.
Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids02:04

Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids

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.

You might also read

Related Articles

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

Sort by
Same author

Million-Fold Activation of C-H Bonds by Fluorinated Nonheme Fe<sup>IV</sup>=O Complexes <i>via</i> Second Sphere Equatorial Substitution and Catalytic Epoxidation to Boot.

ACS catalysis·2026
Same author

Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.

Nature methods·2026
Same author

High-resolution in-beam video rate imaging with the ClearXCam for synchrotron beamlines.

Journal of synchrotron radiation·2026
Same author

Hydroxyl radical footprinting modification reveals an intradomain communication pathway in EFL1 disrupted by a Shwachman-Diamond syndrome-associated mutation.

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

Utilization of Grape Pomace as A Value-added Phenolic Component for Oat Milk Production.

Plant foods for human nutrition (Dordrecht, Netherlands)·2025
Same author

Mimicking sMMOH chemistry: trapping the Sc<sup>3+</sup>-bound nonheme Fe<sup>III</sup>-O-O-Fe<sup>III</sup> adduct prior to its conversion into an Fe<sup>IV</sup> <sub>2</sub>(μ-O)<sub>2</sub> core.

Chemical science·2025
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
Same journal

The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide.

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

Related Experiment Video

Updated: Jun 6, 2026

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase.

Andrew J Fielding1, Elena G Kovaleva, Erik R Farquhar

  • 1Department of Chemistry, Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street, Minneapolis, MN 55455, USA.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|December 15, 2010
PubMed
Summary
This summary is machine-generated.

Homoprotocatechuate 2,3-dioxygenase (HPCD) activity is maintained with manganese or cobalt, despite cobalt's higher redox potential. Metal substitution alters catalytic intermediates, showing dioxygenase catalysis is efficient across various metal redox potentials.

More Related Videos

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
10:14

Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase

Published on: November 8, 2019

Related Experiment Videos

Last Updated: Jun 6, 2026

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
10:14

Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase

Published on: November 8, 2019

Area of Science:

  • Biochemistry
  • Enzymology
  • Metalloprotein research

Background:

  • Homoprotocatechuate 2,3-dioxygenase (HPCD) from Brevibacterium fuscum contains an Fe(II) active site.
  • This active site metal can be substituted with Mn(II) or Co(II).

Purpose of the Study:

  • To investigate the kinetic and structural effects of substituting the Fe(II) center in HPCD with Mn(II) or Co(II).
  • To understand how metal redox potential influences dioxygenase catalysis and O(2) activation mechanisms.

Main Methods:

  • Steady-state kinetic analysis of Fe-HPCD, Mn-HPCD, and Co-HPCD.
  • X-ray crystallography of resting and substrate-bound forms of the metalloenzymes.

Main Results:

  • Mn-HPCD kinetics are similar to Fe-HPCD, while Co-HPCD shows significantly higher catalytic activity ([Formula: see text] and kcat).
  • Structural analysis reveals no changes in the active site or protein structure upon metal substitution.
  • Kinetic data suggest Co(II) alters intermediate interconversion rates but maintains efficient catalysis.

Conclusions:

  • Bacterial dioxygenase catalysis can occur efficiently over a broad range of metal redox potentials.
  • The protein structure does not appear to differentially tune the metal center's potential.
  • Kinetic and spectroscopic properties of Co-HPCD offer insights into extradiol dioxygenase O(2) activation.