scholarly journals The N-terminal sequence of the extrinsic PsbP protein modulates the redox potential of Cyt b559 in photosystem II

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Taishi Nishimura ◽  
Ryo Nagao ◽  
Takumi Noguchi ◽  
Jon Nield ◽  
Fumihiko Sato ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Redox Potential ◽  
Terminal Sequence ◽  
Psbp Protein

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.

scholarly journals Redox potential of pheophytin a in photosystem II of two cyanobacteria having the different special pair chlorophylls

2010 ◽  
Vol 107 (8) ◽  
pp. 3924-3929 ◽  
Author(s):  
Suleyman I. Allakhverdiev ◽  
Tatsuya Tomo ◽  
Yuichiro Shimada ◽  
Hayato Kindo ◽  
Ryo Nagao ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Redox Potential ◽  
Pheophytin A ◽  
Special Pair

The effects of simultaneous RNAi suppression of PsbO and PsbP protein expression in photosystem II of Arabidopsis

2008 ◽  
Vol 98 (1-3) ◽  
pp. 439-448 ◽  
Author(s):  
Xiaoping Yi ◽  
Stefan R. Hargett ◽  
Laurie K. Frankel ◽  
Terry M. Bricker
Keyword(s):  
Photosystem Ii ◽  
Protein Expression ◽  
Psbp Protein

scholarly journals Crystal Structure Analysis of Extrinsic PsbP Protein of Photosystem II Reveals a Manganese-Induced Conformational Change

2015 ◽  
Vol 8 (4) ◽  
pp. 664-666 ◽  
Author(s):  
Peng Cao ◽  
Yuan Xie ◽  
Mei Li ◽  
Xiaowei Pan ◽  
Hongmei Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Conformational Change ◽  
Structure Analysis ◽  
Crystal Structure Analysis ◽  
Psbp Protein

Excitation pressure regulates the activation energy for recombination events in the photosystem II reaction centres of Chlamydomonas reinhardtii

2007 ◽  
Vol 85 (6) ◽  
pp. 721-729 ◽  
Author(s):  
Tessa Pocock ◽  
P. V. Sane ◽  
S. Falk ◽  
N. P.A. Hüner
Keyword(s):  
Activation Energy ◽  
Photosystem Ii ◽  
Redox Potential ◽  
Chlamydomonas Reinhardtii ◽  
Reaction Center ◽  
Growth Conditions ◽  
High Irradiance ◽  
Reaction Centres ◽  
Excitation Pressure

Using in vivo thermoluminescence, we examined the effects of growth irradiance and growth temperature on charge recombination events in photosystem II reaction centres of the model green alga Chlamydomonas reinhardtii. We report that growth at increasing irradiance at either 29 or 15 °C resulted in comparable downward shifts in the temperature peak maxima (TM) for S2QB– charge pair recombination events, with minimal changes in S2QA– recombination events. This indicates that such growth conditions decrease the activation energy required for S2QB– charge pair recombination events with no concomitant change in the activation energy for S2QA– recombination events. This resulted in a decrease in the ΔTM between S2QA– and S2QB– recombination events, which was reversible when shifting cells from low to high irradiance and back to low irradiance at 29 °C. We interpret these results to indicate that the redox potential of QB was modulated independently of QA, which consequently narrowed the redox potential gap between QA and QB in photosystem II reaction centres. Since a decrease in the ΔTM between S2QA– and S2QB– recombination events correlated with growth at increasing excitation pressure, we conclude that acclimation to growth under high excitation pressure narrows the redox potential gap between QA and QB in photosystem II reaction centres, enhancing the probability for reaction center quenching in C. reinhardtii. We discuss the molecular basis for the modulation of the redox state of QB, and suggest that the potential for reaction center quenching complements antenna quenching via the xanthophyll cycle in the photoprotection of C. reinhardtii from excess light.

Are the trapping dynamics in Photosystem II sensitive to QA redox potential?

2001 ◽  
Vol 142 (2-3) ◽  
pp. 127-132 ◽  
Author(s):  
L.M.C Barter ◽  
M.J Schilstra ◽  
J Barber ◽  
J.R Durrant ◽  
D.R Klug
Keyword(s):  
Photosystem Ii ◽  
Redox Potential
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