A Crucial Role of Rh Substituent Ion in Photoinduced Internal Electron Transfer and Enhanced Photocatalytic Activity of CdS-Ti(5.2-x)/6Rhx/2O2Nanohybrids

Small ◽  
2015 ◽  
Vol 11 (43) ◽  
pp. 5771-5780 ◽  
Author(s):  
Jang Mee Lee ◽  
Hyung Bin Jin ◽  
In Young Kim ◽  
Yun Kyung Jo ◽  
Jung-Wook Hwang ◽  
...  
2018 ◽  
Vol 20 (46) ◽  
pp. 29362-29373 ◽  
Author(s):  
Taichi Inagaki ◽  
Norio Takenaka ◽  
Masataka Nagaoka

Electron transfer from both cations and anions to the Au surface contributes dominantly to the electrode potential shift.


1999 ◽  
Vol 274 (38) ◽  
pp. 26956-26961 ◽  
Author(s):  
Tomomasa Shimanuki ◽  
Hideaki Sato ◽  
Simon Daff ◽  
Ikuko Sagami ◽  
Toru Shimizu

2018 ◽  
Vol 6 (11) ◽  
pp. 4768-4775 ◽  
Author(s):  
Mang Wang ◽  
Jinxuan Liu ◽  
Chunmei Guo ◽  
Xiaosu Gao ◽  
Chenghuan Gong ◽  
...  

The two-dimensional ZIF-67 with a leaf-like morphology exhibited the best photocatalytic activity and stability due to the highest CO2 adsorption capability and efficient electron transfer from the excited [Ru(bpy)3]2+ to ZIF-67.


RSC Advances ◽  
2015 ◽  
Vol 5 (72) ◽  
pp. 58184-58190 ◽  
Author(s):  
Meng Wei ◽  
Junmin Wan ◽  
Zhiwen Hu ◽  
Bing Wang ◽  
Zhiqin Peng

Porphyrin plays a crucial role in the process of photocatalysis, porphyrin compounds are naturally suitable antennas for solar energy collection and promising direct solar energy-to-chemical conversion equipment.


2011 ◽  
Vol 435 (1) ◽  
pp. 197-206 ◽  
Author(s):  
Louise Aigrain ◽  
Denis Pompon ◽  
Gilles Truan

CPR (NADPH–cytochrome P450 reductase) is a multidomain protein containing two flavin-containing domains joined by a connecting domain thought to control the necessary movements of the catalytic domains during electronic cycles. We present a detailed biochemical analysis of two chimaeric CPRs composed of the association of human or yeast FMN with the alternative connecting/FAD domains. Despite the assembly of domains having a relatively large evolutionary distance between them, our data support the idea that the integrity of the catalytic cycle is conserved in our chimaeric enzymes, whereas the recognition, interactions and positioning of both catalytic domains are probably modified. The main consequences of the chimaerogenesis are a decrease in the internal electron-transfer rate between both flavins correlated with changes in the geometry of chimaeric CPRs in solution. Results of the present study highlight the role of the linker and connecting domain in the recognition at the interfaces between the catalytic domains and the impact of interdomain interactions on the redox potentials of the flavins, the internal electron-transfer efficiency and the global conformation and dynamic equilibrium of the CPRs.


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