Ligation Of The C-Terminus Of The D1 Polypeptide Of Photosystem Ii To The Oxygen Evolving Complex: A Dft-Qm/Mm Study

2008 ◽  
pp. 363-368 ◽  
Author(s):  
José A. Gascón ◽  
Eduardo M. Sproviero ◽  
James P. McEvoy ◽  
Gary W. Brudvig ◽  
Victor S. Batista
Keyword(s):  
Photosystem Ii ◽  
Oxygen Evolving Complex ◽  
C Terminus ◽  
D1 Polypeptide ◽  
Oxygen Evolving

scholarly journals 13C ENDOR Reveals That the D1 Polypeptide C-Terminus Is Directly Bound to Mn in the Photosystem II Oxygen Evolving Complex

2010 ◽  
Vol 132 (2) ◽  
pp. 446-447 ◽  
Author(s):  
Jamie A. Stull ◽  
Troy A. Stich ◽  
Rachel J. Service ◽  
Richard J. Debus ◽  
Sanjay K. Mandal ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Oxygen Evolving Complex ◽  
C Terminus ◽  
D1 Polypeptide ◽  
Oxygen Evolving

scholarly journals Structural Changes in the Acceptor Site of Photosystem II upon Ca2+/Sr2+ Exchange in the Mn4CaO5 Cluster Site and the Possible Long-Range Interactions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 371
Author(s):  
Koua
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Long Range ◽  
Electron Acceptor ◽  
Structural Changes ◽  
Acceptor Site ◽  
Oxygen Evolving Complex ◽  
Long Range Interactions ◽  
Structural Perturbations ◽  
Oxygen Evolving

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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