Mutagenesis of Basic Residues R151 and R161 in Manganese-Stabilizing Protein of Photosystem II Causes Inefficient Binding of Chloride to the Oxygen-Evolving Complex†

Biochemistry ◽  
2006 ◽  
Vol 45 (9) ◽  
pp. 3107-3115 ◽  
Author(s):  
Hana Popelkova ◽  
Scott D. Betts ◽  
Nikos Lydakis-Symantiris ◽  
Michael M. Im ◽  
Ellen Swenson ◽  
...  

Biochemistry ◽  
2005 ◽  
Vol 44 (24) ◽  
pp. 8817-8825 ◽  
Author(s):  
Wolfgang Gregor ◽  
Roehl M. Cinco ◽  
Hui Yu ◽  
Vittal K. Yachandra ◽  
R. David Britt


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.



2020 ◽  
Vol 118 (21-22) ◽  
pp. e1725168
Author(s):  
K. Yamaguchi ◽  
S. Yamanaka ◽  
H. Isobe ◽  
M. Shoji ◽  
K. Miyagawa ◽  
...  


2005 ◽  
Vol 280 (45) ◽  
pp. 37895-37900 ◽  
Author(s):  
Yukihiro Kimura ◽  
Naoki Mizusawa ◽  
Asako Ishii ◽  
Shigeaki Nakazawa ◽  
Taka-aki Ono






Sign in / Sign up

Export Citation Format

Share Document