ArticleProceedings of the National Academy of Sciences of the United States of America2013
Mechanism of tyrosine D oxidation in Photosystem II.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 78 citations in OpenAlex.
- Asymmetric Connectivity Between Redox-Active Tyrosines and Reaction-Center Chlorophylls in Photosystem II.Plants (Basel, Switzerland) · 2026Article
- Energetics of tryptophan residues in electron transfer and photoprotection of type-II photosynthetic reaction centers.PNAS nexus · 2025Article
- The Effect of Removal of External Proteins PsbO, PsbP and PsbQ on Flash-Induced Molecular Oxygen Evolution and Its Biphasicity in Tobacco PSII.Current issues in molecular biology · 2024Article
- Role of hydrogen-bond networks on the donor side of photosynthetic reaction centers from purple bacteria.Biophysical reviews · 2023Review
- Electron-Transfer Route in the Early Oxidation States of the MnThe journal of physical chemistry. B · 2023Article
- Functional Water Networks in Fully Hydrated Photosystem II.Journal of the American Chemical Society · 2022Article
- Release of a Proton and Formation of a Low-Barrier Hydrogen Bond between Tyrosine D and D2-His189 in Photosystem II.ACS physical chemistry Au · 2022Article
- Binding and functions of the two chloride ions in the oxygen-evolving center of photosystem II.Photosynthesis research · 2022Review
- D139N mutation of PsbP enhances the oxygen-evolving activity of photosystem II through stabilized binding of a chloride ion.PNAS nexus · 2022Article
- HYSCORE and DFT Studies of Proton-Coupled Electron Transfer in a Bioinspired Artificial Photosynthetic Reaction Center.iScience · 2020Article
- Acquirement of water-splitting ability and alteration of the charge-separation mechanism in photosynthetic reaction centers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Extending electron paramagnetic resonance to nanoliter volume protein single crystals using a self-resonant microhelix.Science advances · 2019Article
- Time-Resolved Infrared and Visible Spectroscopy on Cryptochrome aCRY: Basis for Red Light Reception.Biophysical journal · 2019Article
- Unequal misses during the flash-induced advancement of photosystem II: effects of the S state and acceptor side cycles.Photosynthesis research · 2019Article
- 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 · 2019Article
- Energetic insights into two electron transfer pathways in light-driven energy-converting enzymes.Chemical science · 2018Article
- Formation of tyrosine radicals in photosystem II under far-red illumination.Photosynthesis research · 2018Article
- ONature communications · 2018Article
- A novel role for PsbO1 in photosynthetic electron transport as suggested by its light-triggered selective nitration in Arabidopsis thaliana.Plant signaling & behavior · 2018Article
- Genetically introduced hydrogen bond interactions reveal an asymmetric charge distribution on the radical cation of the special-pair chlorophyll P680.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using quantum mechanics/molecular mechanics calculations and the 1.9-Å crystal structure of Photosystem II [Umena Y, Kawakami K, Shen J-R, Kamiya N (2011) Nature 473(7345):55-60], we investigated the H-bonding environment of the redox-active tyrosine D (TyrD) and obtained insights that help explain its slow redox kinetics and the stability of TyrD(•). The water molecule distal to TyrD, located ~4 Å away from the phenolic O of TyrD, corresponds to the presence of the tyrosyl radical state. The water molecule proximal to TyrD, in H-bonding distance to the phenolic O of TyrD, corresponds to the presence of the unoxidized tyrosine. The H(+) released on oxidation of TyrD is transferred to the proximal water, which shifts to the distal position, triggering a concerted proton transfer pathway involving D2-Arg180 and a series of waters, through which the proton reaches the aqueous phase at D2-His61. The water movement linked to the ejection of the proton from the hydrophobic environment near TyrD makes oxidation slow and quasiirreversible, explaining the great stability of the TyrD(•). A symmetry-related proton pathway associated with tyrosine Z is pointed out, and this is associated with one of the Cl(-) sites. This may represent a proton pathway functional in the water oxidation cycle.
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