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Water oxidation in photosystem II

Biological water oxidation, performed by a single enzyme, photosystem II, is a central research topic not only in understanding the photosynthetic apparatus but also for the development of water splitting catalysts for technological applications. Great progress has been made in this endeavor followi...

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Autores principales: Lubitz, Wolfgang, Chrysina, Maria, Cox, Nicholas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6763417/
https://www.ncbi.nlm.nih.gov/pubmed/31187340
http://dx.doi.org/10.1007/s11120-019-00648-3
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author Lubitz, Wolfgang
Chrysina, Maria
Cox, Nicholas
author_facet Lubitz, Wolfgang
Chrysina, Maria
Cox, Nicholas
author_sort Lubitz, Wolfgang
collection PubMed
description Biological water oxidation, performed by a single enzyme, photosystem II, is a central research topic not only in understanding the photosynthetic apparatus but also for the development of water splitting catalysts for technological applications. Great progress has been made in this endeavor following the report of a high-resolution X-ray crystallographic structure in 2011 resolving the cofactor site (Umena et al. in Nature 473:55–60, 2011), a tetra-manganese calcium complex. The electronic properties of the protein-bound water oxidizing Mn(4)O(x)Ca complex are crucial to understand its catalytic activity. These properties include: its redox state(s) which are tuned by the protein matrix, the distribution of the manganese valence and spin states and the complex interactions that exist between the four manganese ions. In this short review we describe how magnetic resonance techniques, particularly EPR, complemented by quantum chemical calculations, have played an important role in understanding the electronic structure of the cofactor. Together with isotope labeling, these techniques have also been instrumental in deciphering the binding of the two substrate water molecules to the cluster. These results are briefly described in the context of the history of biological water oxidation with special emphasis on recent work using time resolved X-ray diffraction with free electron lasers. It is shown that these data are instrumental for developing a model of the biological water oxidation cycle.
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spelling pubmed-67634172019-10-07 Water oxidation in photosystem II Lubitz, Wolfgang Chrysina, Maria Cox, Nicholas Photosynth Res Review Biological water oxidation, performed by a single enzyme, photosystem II, is a central research topic not only in understanding the photosynthetic apparatus but also for the development of water splitting catalysts for technological applications. Great progress has been made in this endeavor following the report of a high-resolution X-ray crystallographic structure in 2011 resolving the cofactor site (Umena et al. in Nature 473:55–60, 2011), a tetra-manganese calcium complex. The electronic properties of the protein-bound water oxidizing Mn(4)O(x)Ca complex are crucial to understand its catalytic activity. These properties include: its redox state(s) which are tuned by the protein matrix, the distribution of the manganese valence and spin states and the complex interactions that exist between the four manganese ions. In this short review we describe how magnetic resonance techniques, particularly EPR, complemented by quantum chemical calculations, have played an important role in understanding the electronic structure of the cofactor. Together with isotope labeling, these techniques have also been instrumental in deciphering the binding of the two substrate water molecules to the cluster. These results are briefly described in the context of the history of biological water oxidation with special emphasis on recent work using time resolved X-ray diffraction with free electron lasers. It is shown that these data are instrumental for developing a model of the biological water oxidation cycle. Springer Netherlands 2019-06-11 2019 /pmc/articles/PMC6763417/ /pubmed/31187340 http://dx.doi.org/10.1007/s11120-019-00648-3 Text en © The Author(s) 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Review
Lubitz, Wolfgang
Chrysina, Maria
Cox, Nicholas
Water oxidation in photosystem II
title Water oxidation in photosystem II
title_full Water oxidation in photosystem II
title_fullStr Water oxidation in photosystem II
title_full_unstemmed Water oxidation in photosystem II
title_short Water oxidation in photosystem II
title_sort water oxidation in photosystem ii
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6763417/
https://www.ncbi.nlm.nih.gov/pubmed/31187340
http://dx.doi.org/10.1007/s11120-019-00648-3
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