ArticlePhotosynthesis research2005
Reaction pattern of photosystem II: oxidative water cleavage and protein flexibility.
Article in Photosynthesis research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- The Effective Force Constant Approach of Protein Flexibility Applied to Selected Photosynthetic Protein Complexes.Molecules (Basel, Switzerland) · 2026Review
- Recent Progress in Solution Structure Studies of Photosynthetic Proteins Using Small-Angle Scattering Methods.Molecules (Basel, Switzerland) · 2023Review
- In memory of Vladimir Anatolievich Shuvalov (1943-2022): an outstanding biophysicist.Photosynthesis research · 2022Article
- Photochemically induced dynamic nuclear polarization NMR on photosystem II: donor cofactor observed in entire plant.Scientific reports · 2018Article
- Solution structure of monomeric and trimeric photosystem I of Thermosynechococcus elongatus investigated by small-angle X-ray scattering.Photosynthesis research · 2017Article
- The plastoquinol-plastoquinone exchange mechanism in photosystem II: insight from molecular dynamics simulations.Photosynthesis research · 2017Article
- Oxidative photosynthetic water splitting: energetics, kinetics and mechanism.Photosynthesis research · 2007Review
- Structural characterization of mumps virus fusion protein core.Biochemical and biophysical research communications · 2006Article
- Photosystem II: structure and mechanism of the water:plastoquinone oxidoreductase.Photosynthesis researchReview
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This short communication addresses three topics of photosynthetic water cleavage in Photosystem II (PS II): (a) effect of protonation in the acidic range on the extent of the 'fast' ns kinetics of P680+. reduction by YZ, (b) mechanism of O-O bond formation and (c) role of protein flexibility in the functional integrity of PS II. Based on measurements of light-induced absorption changes and quasielastic neutron scattering in combination with mechanistic considerations, evidence is presented for the protein acting as a functionally active constituent of the water cleavage machinery, in particular, for directed local proton transfer. A specific flexibility emerging above a threshold of about 230 K is an indispensable prerequisite for oxygen evolution and plastoquinol formation.
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Registered trials
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