ArticleProceedings of the National Academy of Sciences of the United States of America2012
A hydrogen-bonding network plays a catalytic role in photosynthetic oxygen evolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 51 citations in OpenAlex.
- Review
- Quantum Mechanical Assessment of Protein-Ligand Hydrogen Bond Strength Patterns: Insights from Semiempirical Tight-Binding and Local Vibrational Mode Theory.International journal of molecular sciences · 2023Article
- Does Oxygen Feature Chalcogen Bonding?Molecules (Basel, Switzerland) · 2019Article
- Hydroxyectoine protects Mn-depleted photosystem II against photoinhibition acting as a source of electrons.Photosynthesis research · 2019Article
- Thermodynamics of Proton and Electron Transfer in Tetranuclear Clusters with Mn-OHJournal of the American Chemical Society · 2018Article
- Calcium, conformational selection, and redox-active tyrosine YZ in the photosynthetic oxygen-evolving cluster.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Rapid Sampling of Hydrogen Bond Networks for Computational Protein Design.Journal of chemical theory and computation · 2018Article
- Water is an active matrix of life for cell and molecular biology.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Synthetic control and empirical prediction of redox potentials for CoChemical science · 2017Article
- An intrinsically disordered photosystem II subunit, PsbO, provides a structural template and a sensor of the hydrogen-bonding network in photosynthetic water oxidation.The Journal of biological chemistry · 2013Article
- Proton transport facilitating water-oxidation: the role of second sphere ligands surrounding the catalytic metal cluster.Photosynthesis research · 2013Review
- Rescue of deleterious mutations by the compensatory Y30F mutation in ketosteroid isomerase.Molecules and cells · 2013Article
- Detection of an intermediary, protonated water cluster in photosynthetic oxygen evolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural implications of hydrogen-bond energetics in membrane proteins revealed by high-pressure spectroscopy.Biophysical journal · 2012Article
- Assembly and properties of heterobimetallic Co(II/III)/Ca(II) complexes with aquo and hydroxo ligands.Journal of the American Chemical Society · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In photosystem II, oxygen evolution occurs by the accumulation of photo-induced oxidizing equivalents at the oxygen-evolving complex (OEC). The sequentially oxidized states are called the S(0)-S(4) states, and the dark stable state is S(1). Hydrogen bonds to water form a network around the OEC; this network is predicted to involve multiple peptide carbonyl groups. In this work, we tested the idea that a network of hydrogen bonded water molecules plays a catalytic role in water oxidation. As probes, we used OEC peptide carbonyl frequencies, the substrate-based inhibitor, ammonia, and the sugar, trehalose. Reaction-induced FT-IR spectroscopy was used to describe the protein dynamics associated with the S(1) to S(2) transition. A shift in an amide CO vibrational frequency (1664 (S(1)) to 1653 (S(2)) cm(-1)) was observed, consistent with an increase in hydrogen bond strength when the OEC is oxidized. Treatment with ammonia/ammonium altered these CO vibrational frequencies. The ammonia-induced spectral changes are attributed to alterations in hydrogen bonding, when ammonia/ammonium is incorporated into the OEC hydrogen bond network. The ammonia-induced changes in CO frequency were reversed or blocked when trehalose was substituted for sucrose. This trehalose effect is attributed to a displacement of ammonia molecules from the hydrogen bond network. These results imply that ammonia, and by extension water, participate in a catalytically essential hydrogen bond network, which involves OEC peptide CO groups. Comparison to the ammonia transporter, AmtB, reveals structural similarities with the bound water network in the OEC.
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