Unveiling Role of Sulfate Ion in Nickel‐Iron (oxy)Hydroxide with Enhanced Oxygen‐Evolving Performance

2021 ◽  
pp. 2102772
Author(s):  
Hanxiao Liao ◽  
Tao Luo ◽  
Pengfei Tan ◽  
Kejun Chen ◽  
Lili Lu ◽  
...  
Author(s):  
Keisuke Saito ◽  
Minesato Nakagawa ◽  
Manoj Mandal ◽  
Hiroshi Ishikita

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.


Author(s):  
Naoki Mizusawa ◽  
Isamu Sakurai ◽  
Hisako Kubota ◽  
Hajime Wada

2019 ◽  
Vol 11 (51) ◽  
pp. 48002-48012 ◽  
Author(s):  
Michele Orlandi ◽  
Serena Berardi ◽  
Alberto Mazzi ◽  
Stefano Caramori ◽  
Rita Boaretto ◽  
...  

1993 ◽  
Vol 48 (3-4) ◽  
pp. 174-178 ◽  
Author(s):  
Kazuhiko Satoh ◽  
Yasuhiro Kashino ◽  
Hiroyuki Koike

Abstract We have recently shown that binding affinities of benzoquinones can be estimated by two methods in photosystem (PS) II particles (K. Satoh et al., Biochim. Biophys. Acta 1102, 45-52 (1992)). Using these methods we calculated the binding affinity of thymoquinone (2-methyl-5-isopropyl-p-benzoquinone) to the QB site and studied how the quinone accepts electrons in oxygen-evolving PS II particles isolated from the thermophilic cyanobacteria, Synechococcus elongatus and S. vulcanus. The results are as follows: (1) The binding constant of thymoqui­ none to the QB site determined by several methods was around 0.33 mᴍ . (2) At low thymoquinone concentrations the quinone was supposed to accept electrons via QB-plastoquinone, whereas at high concentrations the quinone seemed to bind to the QB site and accept an electron directly from Q-A. Lower rates of photoreduction of the quinone at high concentrations were attributed to a slower turnover rate of the quinone at the QB site than that of endogenous plastoquinone. (3) A model for the function of plastoquinone at the QB site, which can explain all the results, was presented. According to this model, the plastoquinone molecule at the QB site is not replaced by another plastoquinone molecule. Instead, it transfers electrons to pool plastoquinone molecules by turning over its head group but remaining its long side chain bound to the PS II complexes.


1991 ◽  
Vol 43 (2-3) ◽  
pp. 365
Author(s):  
A. Boussac ◽  
P. Sétif ◽  
A.W. Rutherford

1992 ◽  
Vol 21 (1) ◽  
pp. 603-611
Author(s):  
D. Li ◽  
F. Cosandey ◽  
G. E. Maurer ◽  
R. Foote ◽  
J. K. Tien

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