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 Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.6K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
8.6K
The Z-Scheme of Electron Transport in Photosynthesis01:34

The Z-Scheme of Electron Transport in Photosynthesis

10.5K
The light reactions of photosynthesis assume a linear flow of electrons from water to NADP+. During this process, light energy drives the splitting of water molecules to produce oxygen. However, oxidation of water molecules is a thermodynamically unfavorable reaction and requires a strong oxidizing agent. This is accomplished by the first product of light reactions: oxidized P680 (or P680+), the most powerful oxidizing agent known in biology. The oxidized P680 that acquires an electron from the...
10.5K
The Antenna Complex01:15

The Antenna Complex

6.2K
Plants and other photosynthetic organisms comprise pigments capable of absorption of direct sunlight. These pigments are present in the reaction center - the main site of photochemical reactions as well as in the antenna complex. Under average light conditions, the rate at which reaction center pigments absorb light is far below the electron transport chain's capacity. As a result, the reaction center alone cannot provide enough energy to drive photosynthesis. The photosynthetic efficiency can...
6.2K
Photosystem I01:27

Photosystem I

64.4K
Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...
64.4K
Photosystem II01:22

Photosystem II

72.6K
The multi-protein complex photosystem II (PS II) harvests photons and transfers their energy through its bound pigments to its reaction center, and ultimately to photosystem I (PSI) through the electron transport chain. The pigments responsible for caputirng the light energy in photosystems include chlorophyll a, chlorophyll b, and carotenoids.
The pigment molecules are arranged across  two photosystem domains — the antenna complex and the reaction center. The main aim of the pigment...
72.6K
Photosystems01:32

Photosystems

5.0K
Photosystems are multiprotein complexes that form the functional units of photosynthesis in plants, algae, and cyanobacteria. They are found embedded in the membrane of tiny sac-like structures called thylakoids placed inside the chloroplast.
Functioning of Photosystems
Photosystems contain many pigment molecules, such as chlorophylls and carotenoids, arranged in a particular organization across two domains — the antenna complex and the reaction center. The main aim of the pigment...
5.0K

You might also read

Related Articles

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

Sort by
Same author

Identification of a mechanism-based binding mode for a histone deacetylase 6 inhibitor.

Nature communications·2026
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

Fe-Incorporated Co <sub><b>3</b></sub> O <sub><b>4</b></sub> Microsheets for Oxygen Evolution at High Current Densities in All-Platinum-Group-Metal-Free Alkaline Anion Exchange Membrane Electrolyzers.

ACS applied energy materials·2026
Same author

Bicyclo[1.1.1]pentane Ketones via Friedel-Crafts Acylation.

The Journal of organic chemistry·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 author

Synthesis, Computational Studies, and Structural Analysis of 1-(3,5-Dimethoxyphenyl)azetidin-2-ones with Antiproliferative Activity in Breast Cancer and Chemoresistant Colon Cancer.

Pharmaceuticals (Basel, Switzerland)·2025

Related Experiment Video

Updated: Sep 13, 2025

Characterizing Electron Transport through Living Biofilms
08:52

Characterizing Electron Transport through Living Biofilms

Published on: June 1, 2018

8.5K

Electrostatic Fields Induce Accelerated Proton Coupled Electron Transfer Rates in Chlorophyll Model Compounds.

Oscar Reid Kelly1, Brendan Twamley1, Marcel Swart2,3

  • 1School of Chemistry, Trinity College Dublin, The University of Dublin, College Green, Dublin 2, Ireland.

Journal of the American Chemical Society
|July 29, 2025
PubMed
Summary
This summary is machine-generated.

Electrostatic fields tune chlorophyll model compound redox potentials. Cation binding increases oxidative reactivity, mimicking crucial photosynthesis electron transfer processes.

More Related Videos

Evaluation of Photosynthetic Behaviors by Simultaneous Measurements of Leaf Reflectance and Chlorophyll Fluorescence Analyses
10:20

Evaluation of Photosynthetic Behaviors by Simultaneous Measurements of Leaf Reflectance and Chlorophyll Fluorescence Analyses

Published on: August 9, 2019

12.8K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.3K

Related Experiment Videos

Last Updated: Sep 13, 2025

Characterizing Electron Transport through Living Biofilms
08:52

Characterizing Electron Transport through Living Biofilms

Published on: June 1, 2018

8.5K
Evaluation of Photosynthetic Behaviors by Simultaneous Measurements of Leaf Reflectance and Chlorophyll Fluorescence Analyses
10:20

Evaluation of Photosynthetic Behaviors by Simultaneous Measurements of Leaf Reflectance and Chlorophyll Fluorescence Analyses

Published on: August 9, 2019

12.8K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.3K

Area of Science:

  • Biophysical Chemistry
  • Photochemistry
  • Photosynthesis Research

Background:

  • Chlorophyll pigments are vital for photosynthesis, acting as primary electron donors.
  • Significant variation in chlorophyll redox potentials (0.5-1.3 V vs SHE) exists, with limited experimental understanding.
  • Understanding redox potential origins is key to elucidating photosynthetic electron transfer mechanisms.

Purpose of the Study:

  • To investigate the influence of electrostatic fields on the redox potentials of chlorophyll model compounds.
  • To synthesize and characterize Mg-porphyrin complexes as chlorophyll analogs.
  • To explore how cation binding affects the reactivity of oxidized chlorophyll models.

Main Methods:

  • Synthesis of crown ether-appended Mg-porphyrin complexes.
  • Characterization using UV-vis, FT-IR, EPR spectroscopies, and ESI-MS.
  • Investigation of cation binding effects on redox potentials and reaction rates.

Main Results:

  • Cation binding to Mg-porphyrin complexes linearly increased redox potentials via an electrostatic field effect.
  • Synthesized π-cation radical complexes mimicked photo-oxidized chlorophyll in reactivity.
  • Cation binding enhanced the rates of proton-coupled electron transfer (PCET) and electron transfer (ET) reactions.

Conclusions:

  • Electrostatic fields are a significant factor in tuning the redox potentials of chlorophyll model compounds.
  • This study provides experimental evidence for electrostatic control over photosynthetic electron donor reactivity.
  • Findings offer insights into optimizing artificial photosynthetic systems and understanding natural photosynthesis.