Selenium vacancy triggered atomic disordering of Co0.85Se nanoparticles towards a highly-active electrocatalyst for water oxidation

2020 ◽  
Vol 56 (92) ◽  
pp. 14451-14454
Author(s):  
Jiahao Zhang ◽  
Qiucheng Xu ◽  
Yanjie Hu ◽  
Hao Jiang ◽  
Chunzhong Li

A moderate VSe degree can optimize the atomic disordering and electronic structure of Co-centers, remarkably enhancing the alkaline OER performance of Co0.85Se.

Author(s):  
Shuya Zhao ◽  
Yurui Xue ◽  
Zhongqiang Wang ◽  
Zhiqiang Zheng ◽  
Xiaoyu Luan ◽  
...  

Developing highly active, stable and low-cost electrocatalysts capable of an efficient oxygen evolution reaction (OER) is urgent and challenging.


2008 ◽  
Vol 47 (21) ◽  
pp. 3896-3899 ◽  
Author(s):  
Yurii V. Geletii ◽  
Bogdan Botar ◽  
Paul Kögerler ◽  
Daniel A. Hillesheim ◽  
Djamaladdin G. Musaev ◽  
...  

2018 ◽  
Vol 57 (28) ◽  
pp. 8396-8415 ◽  
Author(s):  
Jeongsuk Seo ◽  
Hiroshi Nishiyama ◽  
Taro Yamada ◽  
Kazunari Domen

ChemSusChem ◽  
2014 ◽  
Vol 7 (8) ◽  
pp. 2202-2211 ◽  
Author(s):  
Prashanth W. Menezes ◽  
Arindam Indra ◽  
Patrick Littlewood ◽  
Michael Schwarze ◽  
Caren Göbel ◽  
...  

Author(s):  
Xiaojue Bai ◽  
Wenxiu He ◽  
Xingyu Lu ◽  
Yu Fu ◽  
Wei Qi

The rational design and exploitation of highly active and stable catalysts for the electrochemical oxidation of biomass-derived 5-hydroxymethylfurfural (HMF) to valuable chemical 2,5-furandi-carboxylic acid (FDCA), is of great significance. Herein,...


2018 ◽  
Vol 43 (50) ◽  
pp. 22529-22537 ◽  
Author(s):  
Xiaona Ren ◽  
Fang Hou ◽  
Fangyuan Wang ◽  
Xiangwen Zhang ◽  
Qingfa Wang

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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