An ESEEM study of the oxidized electron donor of plant photosystem II: Evidence that D is a neutral tyrosine radical
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Reference22 articles.
1. In the oxygen-evolving complex of photosystem II the S0 state is oxidized to the S1 state by D+ (signal IIslow)
2. Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system.
3. Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: Donor D is a tyrosine residue in the D2 protein
4. Electron paramagnetic resonance Signal II in spinach chloroplasts. II. Alternative spectral forms and inhibitor effects on kinetics of Signal II in flashing light
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2. Microsolvation of the Redox-Active Tyrosine-D in Photosystem II: Correlation of Energetics with EPR Spectroscopy and Oxidation-Induced Proton Transfer;Journal of the American Chemical Society;2019-01-22
3. Elucidating the design principles of photosynthetic electron-transfer proteins by site-directed spin labeling EPR spectroscopy;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2016-05
4. Advanced Electron Paramagnetic Resonance Studies of the Oxygen-Evolving Complex;Metalloproteins;2015-04-15
5. Spectroscopic Evidence for a Redox-Controlled Proton Gate at Tyrosine D in Photosystem II;Biochemistry;2014-09-05
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