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A five-coordinate Mn(IV) intermediate in biological water oxidation: spectroscopic signature and a pivot mechanism for water binding
Max Planck Inst Chem Energy Convers, D-45470 Mulheim, Germany..
Max Planck Inst Chem Energy Convers, D-45470 Mulheim, Germany..
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Max Planck Inst Chem Energy Convers, D-45470 Mulheim, Germany..
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2016 (English)In: Chemical Science, ISSN 2041-6520, E-ISSN 2041-6539, Vol. 7, no 1, 72-84 p.Article in journal (Refereed) PublishedText
Abstract [en]

Among the four photo-driven transitions of the water-oxidizing tetramanganese-calcium cofactor of biological photosynthesis, the second-last step of the catalytic cycle, that is the S-2 to S-3 state transition, is the crucial step that poises the catalyst for the final O-O bond formation. This transition, whose intermediates are not yet fully understood, is a multi-step process that involves the redox-active tyrosine residue and includes oxidation and deprotonation of the catalytic cluster, as well as the binding of a water molecule. Spectroscopic data has the potential to shed light on the sequence of events that comprise this catalytic step, which still lacks a structural interpretation. In this work the S-2-S-3 state transition is studied and a key intermediate species is characterized: it contains a Mn3O4Ca cubane subunit linked to a five-coordinate Mn(IV) ion that adopts an approximately trigonal bipyramidal ligand field. It is shown using high-level density functional and multireference wave function calculations that this species accounts for the near-infrared absorption and electron paramagnetic resonance observations on metastable S-2-S-3 intermediates. The results confirm that deprotonation and Mn oxidation of the cofactor must precede the coordination of a water molecule, and lead to identification of a novel low-energy water binding mode that has important implications for the identity of the substrates in the mechanism of biological water oxidation.

Place, publisher, year, edition, pages
2016. Vol. 7, no 1, 72-84 p.
National Category
Chemical Sciences
URN: urn:nbn:se:uu:diva-274423DOI: 10.1039/c5sc03124aISI: 000366826900005OAI: diva2:896551
Swedish Research CouncilKnut and Alice Wallenberg FoundationSwedish Energy Agency
Available from: 2016-01-21 Created: 2016-01-21 Last updated: 2016-04-21Bibliographically approved

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