ArticleBiochemistry2014
Pulse electron paramagnetic resonance studies of the interaction of methanol with the S2 state of the Mn4O5Ca cluster of photosystem II.
Article in Biochemistry, 2014. 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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Who cites it
15 citing papers in PubMed, 47 citations in OpenAlex.
- Electronic Structure of the SACS physical chemistry Au · 2025Article
- Ammonia Binding to the Oxygen-Evolving Complex Probed by High-Energy Resolution Fluorescence Detected X-Ray Absorption Spectroscopy.The journal of physical chemistry. B · 2025Article
- The SPhotosynthesis research · 2024Article
- Comprehensive Evaluation of Models for Ammonia Binding to the Oxygen Evolving Complex of Photosystem II.The journal of physical chemistry. B · 2024Article
- Evolutionary diversity of proton and water channels on the oxidizing side of photosystem II and their relevance to function.Photosynthesis research · 2023Review
- Functional Water Networks in Fully Hydrated Photosystem II.Journal of the American Chemical Society · 2022Article
- The exchange of the fast substrate water in the SChemical science · 2021Article
- CaMnAngewandte Chemie (International ed. in English) · 2021Article
- Arrested Substrate Binding Resolves Catalytic Intermediates in Higher-Plant Water Oxidation.Angewandte Chemie (International ed. in English) · 2021Article
- Water oxidation in photosystem II.Photosynthesis research · 2019Review
- Five-coordinate MnProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Tetranuclear [MnJournal of the American Chemical Society · 2018Article
- Thermodynamics of Proton and Electron Transfer in Tetranuclear Clusters with Mn-OHJournal of the American Chemical Society · 2018Article
- Theoretical study of the EPR spectrum of the SPhotosynthesis research · 2016Article
- Interaction of methanol with the oxygen-evolving complex: atomistic models, channel identification, species dependence, and mechanistic implications.Chemical science · 2016Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The binding of the substrate analogue methanol to the catalytic Mn4CaO5 cluster of the water-oxidizing enzyme photosystem II is known to alter the electronic structure properties of the oxygen-evolving complex without retarding O2-evolution under steady-state illumination conditions. We report the binding mode of (13)C-labeled methanol determined using 9.4 GHz (X-band) hyperfine sublevel-correlation (HYSCORE) and 34 GHz (Q-band) electron spin-echo electron nuclear double resonance (ESE-ENDOR) spectroscopies. These results are compared to analogous experiments on a mixed-valence Mn(III)Mn(IV) complex (2-OH-3,5-Cl2-salpn)2Mn(III)Mn(IV) (salpn = N,N'-bis(3,5-dichlorosalicylidene)-1,3-diamino-2-hydroxypropane) in which methanol ligates to the Mn(III) ion ( Larson et al. (1992) J. Am. Chem. Soc. , 114 , 6263 ). In the mixed-valence Mn(III,IV) complex, the hyperfine coupling to the (13)C of the bound methanol (Aiso = 0.65 MHz, T = 1.25 MHz) is appreciably larger than that observed for (13)C methanol associated with the Mn4CaO5 cluster poised in the S2 state, where only a weak dipolar hyperfine interaction (Aiso = 0.05 MHz, T = 0.27 MHz) is observed. An evaluation of the (13)C hyperfine interaction using the X-ray structure coordinates of the Mn4CaO5 cluster indicates that methanol does not bind as a terminal ligand to any of the manganese ions in the oxygen-evolving complex. We favor methanol binding in place of a water ligand to the Ca(2+) in the Mn4CaO5 cluster or in place of one of the waters that form hydrogen bonds with the oxygen bridges of the cluster.
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