Water oxidation in photosystem II
Date
2019-10
Authors
Lubitz, Wolfgang
Chrysina, Maria
Cox, Nicholas
Journal Title
Journal ISSN
Volume Title
Publisher
Springer Verlag
Abstract
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 Mn4OxCa 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.
Description
Keywords
epr spectroscopy, oxygen-evolving complex, photosystem ii, quantum chemical calculations, triplet oxygen formation, water binding, bacterial proteins, crystallography, x-ray, cyanobacteria, kinetics, models, biological, models, chemical, models, molecular, oxidation-reduction, oxygen, photosystem ii protein complex, protein structure, tertiary, thermosynechococcus, water
Citation
Collections
Source
Photosynthesis research
Type
Journal article
Book Title
Entity type
Access Statement
Open Access
License Rights
Creative Commons Attribution 4.0 International License