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The Z-Scheme of Electron Transport in Photosynthesis

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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...

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Updated: Jun 23, 2026

Photochemical Oxidative Growth of Iridium Oxide Nanoparticles on CdSe@CdS Nanorods

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Published on: February 11, 2016

New Water Oxidation Mechanism in Photosystem II Resolves Major Experimental Controversies.

Yulia Pushkar¹

¹Department of Physics and Astronomy, Purdue University, West Lafayette, Indiana, USA.

Angewandte Chemie (International Ed. in English)

|June 22, 2026

Summary

Researchers reveal a novel mechanism for oxygen formation in photosystem II, identifying a key oxygen (O3) and its coupling with manganese-bound oxygen (O6) for O-O bond creation.

Keywords:

DFT H‐bond Kok cycle Mn4Ca cluster O─O bond formation mechanism oxygen evolving complex photosystem II

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Published on: October 5, 2019

Area of Science:

Biochemistry
Photosynthesis Research
Bioenergetics

Background:

Photosystem II (PSII) is crucial for oxygenic photosynthesis, sustaining life.
The Mn4CaO5 cluster within PSII catalyzes water oxidation.
Current models struggle to explain O-O bond formation and the protein's role.

Purpose of the Study:

To elucidate the mechanism of O-O bond formation in PSII.
To reconcile experimental data with computational models.
To understand the influence of the protein environment on catalysis.

Main Methods:

Advanced physical techniques were employed.
Computational modeling was utilized.
Analysis focused on the S2 to S3 transition state.

Main Results:

Identified a unique oxygen (O3) ligated by histidine (His337) as a slow-exchanging substrate.
Proposed an O3-O6 peroxide intermediate formed during the S2 to S3 transition.
This pathway is energetically favorable and consistent with experimental data.

Conclusions:

A novel O-O bond formation mechanism involving O3 and O6 is proposed.
The protein environment, via His337, steers catalysis through charge control and Mn1 coordination.
This finding resolves prior discrepancies and offers new avenues for research.