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Hydrogen peroxide as an alternate substrate for the oxygen-evolving complex.

W D Frasch, R Mei

Biochimica Et Biophysica Acta

|March 25, 1987

Summary

Photosystem II reaction centers can evolve oxygen from hydrogen peroxide in the dark. This KCN-insensitive activity is catalyzed by the oxygen-evolving complex

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Characterization of inhibitory effects of NH2OH and its N-methyl derivatives on the O 2-evolving complex of Photosystem II.

Photosynthesis research·2013

Area of Science:

Biochemistry
Photosynthesis research
Plant physiology

Background:

Photosystem II (PSII) reaction centers are known for water oxidation during photosynthesis.
PSII can exhibit oxygen evolution activity using hydrogen peroxide (H2O2) as a substrate in the dark.
A portion of this H2O2-driven O2 evolution is insensitive to potassium cyanide (KCN), suggesting a non-catalase mechanism.

Purpose of the Study:

To investigate the mechanism of KCN-insensitive oxygen evolution from H2O2 in Photosystem II reaction centers.
To provide evidence for the involvement of the oxygen-evolving complex (OEC) and its S-state cycle in this process.

Main Methods:

Utilizing isolated Photosystem II reaction centers.
Assessing oxygen evolution in the dark with H2O2 as a substrate.
Employing KCN to differentiate catalytic activities.
Inactivating the OEC via Ca/EDTA washing.
Testing the effects of inhibitors like ammonia, Tris, and CCCP.
Measuring the dependence on essential cofactors like calcium and chloride.

Main Results:

A significant portion (up to 75%) of H2O2-mediated O2 evolution was insensitive to 1 mM KCN.
This KCN-insensitive activity was abolished by Ca/EDTA washing, indicating OEC involvement.
Ammonia and Tris inhibited the reaction, consistent with OEC-mediated processes.
CCCP, known to affect S2 state stability, also inhibited the activity.
Oxygen evolution rate showed a direct dependence on calcium and chloride concentrations.

Conclusions:

The KCN-insensitive oxygen evolution from H2O2 in the dark is catalyzed by the cycling of S states within the oxygen-evolving complex.
This finding highlights the catalytic versatility of the OEC beyond water oxidation.
The results provide further mechanistic insights into the function of the oxygen-evolving complex.

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