scholarly journals Polypeptides of the oxygen-evolving photosystem II complex. Immunological detection and biogenesis.

1986 ◽  
Vol 261 (12) ◽  
pp. 5296-5300
Author(s):  
V Liveanu ◽  
C F Yocum ◽  
N Nelson
Keyword(s):  
Photosystem Ii ◽  
Immunological Detection ◽  
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

scholarly journals Role of redox-inactive metals in controlling the redox potential of heterometallic manganese–oxido clusters

2021 ◽  
Author(s):  
Keisuke Saito ◽  
Minesato Nakagawa ◽  
Manoj Mandal ◽  
Hiroshi Ishikita
Keyword(s):  
Photosystem Ii ◽  
Redox Potential ◽  
Quantum Chemical Calculations ◽  
Catalytic Reaction ◽  
Quantum Chemical ◽  
Ionic Radius ◽  
Redox Potentials ◽  
Oxygen Evolving ◽  
Highest Occupied Molecular Orbitals

AbstractPhotosystem II (PSII) contains Ca2+, which is essential to the oxygen-evolving activity of the catalytic Mn4CaO5 complex. Replacement of Ca2+ with other redox-inactive metals results in a loss/decrease of oxygen-evolving activity. To investigate the role of Ca2+ in this catalytic reaction, we investigate artificial Mn3[M]O2 clusters redox-inactive metals  [M] ([M]  = Mg2+, Ca2+, Zn2+, Sr2+, and Y3+), which were synthesized by Tsui et al. (Nat Chem 5:293, 2013). The experimentally measured redox potentials (Em) of these clusters are best described by the energy of their highest occupied molecular orbitals. Quantum chemical calculations showed that the valence of metals predominantly affects Em(MnIII/IV), whereas the ionic radius of metals affects Em(MnIII/IV) only slightly.

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