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  Ammonia binding to the oxygen-evolving complex of photosystem II identifies the solvent-exchangeable oxygen bridge (μ-oxo) of the manganese tetramer

Pérez Navarro, M., Ames, W. M., Nilsson, H., Lohmiller, T., Pantazis, D. A., Rapatskiy, L., et al. (2013). Ammonia binding to the oxygen-evolving complex of photosystem II identifies the solvent-exchangeable oxygen bridge (μ-oxo) of the manganese tetramer. Proceedings of the National Academy of Sciences of the United States of America, 110(39), 15561-15566. doi:10.1073/pnas.1304334110.

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 Creators:
Pérez Navarro, Montserrat1, Author           
Ames, William M.2, Author           
Nilsson , Håkan3, Author
Lohmiller, Thomas1, Author           
Pantazis, Dimitrios A.2, Author           
Rapatskiy, Leonid1, Author           
Nowaczyk, Marc M.4, Author
Neese, Frank2, Author           
Boussac, Alain5, Author
Messinger, Johannes3, Author
Lubitz, Wolfgang1, Author           
Cox, Nicholas1, Author           
Affiliations:
1Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023873              
2Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
3Department of Chemistry, Chemical Biological Centre, Umeå University, S-90187 Umeå, Sweden, ou_persistent22              
4Plant Biochemistry, Ruhr-Universität Bochum, D-44780 Bochum, Germany, ou_persistent22              
5iBiTec-S, Centre National de la Recherche Scientifique Unité Mixte de Recherche 8221, Commissariat à l’Energie Atomique Saclay, 91191 Gif-sur-Yvette, France, ou_persistent22              

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 Abstract: The assignment of the two substrate water sites of the tetra-manganese penta-oxygen calcium (Mn4O5Ca) cluster of photosystem II is essential for the elucidation of the mechanism of biological O-O bond formation and the subsequent design of bio-inspired water-splitting catalysts. We recently demonstrated using pulsed EPR spectroscopy that one of the five oxygen bridges (μ-oxo) exchanges unusually rapidly with bulk water and is thus a likely candidate for one of the substrates. Ammonia, a water analog, was previously shown to bind to the Mn4O5Ca cluster, potentially displacing a water/substrate ligand [Britt RD, et al. (1989) J Am Chem Soc 111(10):3522–3532]. Here we show by a combination of EPR and time-resolved membrane inlet mass spectrometry that the binding of ammonia perturbs the exchangeable μ-oxo bridge without drastically altering the binding/exchange kinetics of the two substrates. In combination with broken-symmetry density functional theory, our results show that (i) the exchangable μ-oxo bridge is O5 {using the labeling of the current crystal structure [Umena Y, et al. (2011) Nature 473(7345):55–60]}; (ii) ammonia displaces a water ligand to the outer manganese (MnA4-W1); and (iii) as W1 is trans to O5, ammonia binding elongates the MnA4-O5 bond, leading to the perturbation of the μ-oxo bridge resonance and to a small change in the water exchange rates. These experimental results support O-O bond formation between O5 and possibly an oxyl radical as proposed by Siegbahn and exclude W1 as the second substrate water.

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Language(s): eng - English
 Dates: 2013-03-062013-08-132013-09-102013-09-24
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1304334110
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : PNAS
Source Genre: Journal
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Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 110 (39) Sequence Number: - Start / End Page: 15561 - 15566 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230