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

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
The Electron Transport Chain01:30

The Electron Transport Chain

19.2K
The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
19.2K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

10.2K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
10.2K
Factors Influencing the Rate of Chemical Reactions01:22

Factors Influencing the Rate of Chemical Reactions

7.6K
A variety of factors influence the rate of chemical reactions. For a chemical reaction to happen, atoms must collide with enough energy to overcome the repulsion between their electrons. This energy is called activation energy. Factors influencing the rate of reaction either lower the activation energy or increase the likelihood of a successful collision.
Concentration and Pressure:
The more particles present within a given space, the more likely those particles are to bump into one another....
7.6K
Redox Reactions01:27

Redox Reactions

688
Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
688
Electron Transport Chain Components01:29

Electron Transport Chain Components

699
The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
699

You might also read

Related Articles

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

Sort by
Same author

A Stepwise Thiol Dioxygenation Mechanism in Mercaptosuccinate Dioxygenase Revealed by A Combined Experimental and Computational Study.

bioRxiv : the preprint server for biology·2026
Same author

How Does Tuning of the Primary Coordination Sphere Around Ferryl-Oxo Intermediates Affect Structure and Reactivity? Insights into Axial and Equatorial Ligand Field Effects.

JACS Au·2026
Same author

Secondary-Sphere Hydrogen Bonds Regulating Spin-Redox Interplay in Hemes.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Metal ligand cooperativity in the direct carboxylation and esterification of terminal alkynes by Cu-CNC complexes bearing 2,6-lutidine linkers.

Chemical science·2026
Same author

Computation suggests that the cell adhesion sub-proteome is enriched for sites of pH-dependence and charge burial.

PloS one·2025
Same author

Sulfur-ligated iron(iv)-imido and iron(iv)-oxo complexes, which one is more reactive?

Chemical science·2025

Related Experiment Video

Updated: Dec 12, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K

How Do Metal Ions Modulate the Rate-Determining Electron-Transfer Step in Cytochrome P450 Reactions?

Vaibhav A Dixit1, Jim Warwicker2,3, Sam P de Visser2,4

  • 1Department of Pharmacy, Birla Institute of Technology and Sciences Pilani (BITS-Pilani), Vidya Vihar Campus 41, Pilani, 333031, Rajasthan, India.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|August 8, 2020
PubMed
Summary

Metal and organic ions, solvent, and electric fields significantly alter cytochrome P450 (CYP450) enzyme activity by affecting electron transfer rates. Computational studies suggest active CYP450 forms likely avoid multiple bound alkali metal ions.

Keywords:
Marcus theorydensity functional calculationselectron transferenzyme modelshemeredox potential

More Related Videos

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
06:01

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1

Published on: November 26, 2014

13.8K
Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
05:35

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

7.8K

Related Experiment Videos

Last Updated: Dec 12, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K
EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
06:01

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1

Published on: November 26, 2014

13.8K
Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
05:35

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

7.8K

Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Enzyme kinetics

Background:

  • Cytochrome P450 (CYP450) enzymes are crucial for human health, metabolizing various compounds.
  • The initial electron transfer step in CYP450 reactions is critical for their catalytic activity.
  • Experimental studies indicate that metal ions significantly influence this electron transfer step.

Purpose of the Study:

  • To computationally investigate the impact of external factors on the CYP450 first electron transfer.
  • To understand how metal ions, organic ions, solvent molecules, and electric fields perturb CYP450 activity.
  • To elucidate the relationship between ion interactions and catalytic reaction rates.

Main Methods:

  • Computational modeling of CYP450 with various perturbing agents.
  • Simulation of electron transfer processes in the presence of ions and electric fields.
  • Analysis of reaction driving force and electron transfer rates.

Main Results:

  • Medium-range interactions with ions and electric fields dramatically influence electron transfer driving force and rates.
  • The effect on catalytic rates depends on the location, distance, and orientation of perturbing agents.
  • Calculations on crystal structures revealed inhibitory patterns of bound alkali metal ions.

Conclusions:

  • External perturbations like ions and electric fields significantly modulate CYP450 enzyme activity.
  • Active CYP450 isozymes are predicted to have limited alkali metal ion binding in their second-coordination sphere.
  • This study offers insights into CYP450 regulation and the impact of environmental factors on enzyme function.