Structure of the oxygen-evolving complex of Photosystem II: Calcium and lanthanum compete for sites on the oxidizing side of Photosystem II which control the binding of water-soluble polypeptides and regulate the activity of the manganese complex

1985 ◽  
Vol 809 (2) ◽  
pp. 173-180 ◽  
Author(s):  
Demetrios F. Ghanotakis ◽  
Gerald T. Babcock ◽  
Charles F. Yocum
2019 ◽  
Vol 21 (41) ◽  
pp. 22902-22909
Author(s):  
Christine Mehlich ◽  
Christoph van Wüllen

Broken-symmetry density functional calculations have been used to calculate effective 55Mn hyperfine (A) tensors for a mixed-valence tetranuclear manganese complex, a model system for the S2 state of the oxygen-evolving complex of photosystem II.


Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 371
Author(s):  
Koua

The Mn4CaO5 cluster site in the oxygen-evolving complex (OEC) of photosystem II (PSII) undergoes structural perturbations, such as those induced by Ca2+/Sr2+ exchanges or Ca/Mn removal. These changes have been known to induce long-range positive shifts (between +30 and +150 mV) in the redox potential of the primary quinone electron acceptor plastoquinone A (QA), which is located 40 Å from the OEC. To further investigate these effects, we reanalyzed the crystal structure of Sr-PSII resolved at 2.1 Å and compared it with the native Ca-PSII resolved at 1.9 Å. Here, we focus on the acceptor site and report the possible long-range interactions between the donor, Mn4Ca(Sr)O5 cluster, and acceptor sites.


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