scholarly journals Introduction of Mn(iii) to regulate the electronic structure of fluorine-doped nickel hydroxide for efficient water oxidation

2019 ◽  
Vol 1 (10) ◽  
pp. 4099-4108 ◽  
Author(s):  
Jiaqi Lv ◽  
Xiaoxuan Yang ◽  
Ke Li ◽  
Xinyu Chen ◽  
Sai Sun ◽  
...  

The Mn and F co-doped Ni(OH)2/Ni foam material with rich oxygen defects has excellent OER activity in 1 M KOH.

2022 ◽  
Author(s):  
Xiaoqiang Du ◽  
Jiaxin Li ◽  
Xiaoshuang Zhang

Transition metal materials with high efficiency and durable electrocatalytic water splitting activity have aroused widespread concern among scientists. In this work, two cation co-doped Ni3S4 nanoarrays grown on Ni foam...


2021 ◽  
Author(s):  
Meng-Yang Li ◽  
Jun-Jun Zhang ◽  
Xiang Li ◽  
Weiwei Bao ◽  
Chunming Yang ◽  
...  

Low cost electrodes with high activity and stability are the key to water splitting for green hydrogen production. Herein, an efficient integrated Ni/CoFe LDH array electrocatalyst is synthesized by an...


Author(s):  
Di Li ◽  
Yingying Xing ◽  
Changjian Zhou ◽  
Yikai Lu ◽  
Shengjie Xu ◽  
...  

The high reaction energy barrier of the oxygen evolution reaction (OER) extremely reduces the efficiency of water splitting, which is not conducive to large-scale production of hydrogen. Due to the...


Author(s):  
Lei Zhang ◽  
Xiu-Fei Zhao ◽  
Zhengqiu Yuan ◽  
Ming Wu ◽  
Hu Zhou

Single atom catalysts (SACs) show outstanding activity and selectivity in chemical catalysis owing to its unique electronic structure and unsaturated coordination environment, in which every dispersed metal species on support...


2021 ◽  
Vol 7 (9) ◽  
pp. 131
Author(s):  
Maria Chrysina ◽  
Georgia Zahariou ◽  
Nikolaos Ioannidis ◽  
Yiannis Sanakis ◽  
George Mitrikas

The biological water oxidation takes place in Photosystem II (PSII), a multi-subunit protein located in thylakoid membranes of higher plant chloroplasts and cyanobacteria. The catalytic site of PSII is a Mn4Ca cluster and is known as the oxygen evolving complex (OEC) of PSII. Two tyrosine residues D1-Tyr161 (YZ) and D2-Tyr160 (YD) are symmetrically placed in the two core subunits D1 and D2 and participate in proton coupled electron transfer reactions. YZ of PSII is near the OEC and mediates electron coupled proton transfer from Mn4Ca to the photooxidizable chlorophyll species P680+. YD does not directly interact with OEC, but is crucial for modulating the various S oxidation states of the OEC. In PSII from higher plants the environment of YD• radical has been extensively characterized only in spinach (Spinacia oleracea) Mn- depleted non functional PSII membranes. Here, we present a 2D-HYSCORE investigation in functional PSII of spinach to determine the electronic structure of YD• radical. The hyperfine couplings of the protons that interact with the YD• radical are determined and the relevant assignment is provided. A discussion on the similarities and differences between the present results and the results from studies performed in non functional PSII membranes from higher plants and PSII preparations from other organisms is given.


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