Heterogeneous Composition of Oxygen-Evolving Complexes in Crystal Structures of Dark-Adapted Photosystem II

Biochemistry ◽  
2021 ◽  
Author(s):  
Jimin Wang ◽  
Christopher J. Gisriel ◽  
Krystle Reiss ◽  
Hao-Li Huang ◽  
William H. Armstrong ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Crystal Structures ◽  
Oxygen Evolving

scholarly journals Computational Insights on Crystal Structures of the Oxygen-Evolving Complex of Photosystem II with Either Ca2+ or Ca2+ Substituted by Sr2+

Biochemistry ◽  
2015 ◽  
Vol 54 (3) ◽  
pp. 820-825 ◽  
Author(s):  
Leslie Vogt ◽  
Mehmed Z. Ertem ◽  
Rhitankar Pal ◽  
Gary W. Brudvig ◽  
Victor S. Batista
Keyword(s):  
Photosystem Ii ◽  
Crystal Structures ◽  
Oxygen Evolving Complex ◽  
Oxygen Evolving

Characterization of photosystem II with the atomic-force microscope

1992 ◽  
Vol 50 (2) ◽  
pp. 1146-1147
Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon
Keyword(s):  
Photosystem Ii ◽  
Atomic Force Microscope ◽  
Three Dimensional ◽  
Biologically Active ◽  
Atomic Force ◽  
Freeze Etching ◽  
Image Averaging ◽  
Oxygen Evolving ◽  
Averaging Techniques

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.

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.

scholarly journals Structure of the catalytic, inorganic core of oxygen-evolving photosystem II at 1.9Å resolution

2011 ◽  
Vol 104 (1-2) ◽  
pp. 9-18 ◽  
Author(s):  
Keisuke Kawakami ◽  
Yasufumi Umena ◽  
Nobuo Kamiya ◽  
Jian-Ren Shen
Keyword(s):  
Photosystem Ii ◽  
Oxygen Evolving

Characterization of a resolved oxygen-evolving Photosystem II preparation from spinach thylakoids

1983 ◽  
Vol 724 (2) ◽  
pp. 201-211 ◽  
Author(s):  
Eric Lam ◽  
Barbara Baltimore ◽  
William Ortiz ◽  
Susan Chollar ◽  
Anastasios Melis ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Oxygen Evolving ◽  
Spinach Thylakoids
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