scholarly journals Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a “Bridging Peroxo” Intermediate Involved in Facile 4e–/4H+ O2-Reduction

2015 ◽  
Vol 137 (40) ◽  
pp. 12897-12905 ◽  
Author(s):  
Sudipta Chatterjee ◽  
Kushal Sengupta ◽  
Shabnam Hematian ◽  
Kenneth D. Karlin ◽  
Abhishek Dey
Inorganics ◽  
2019 ◽  
Vol 7 (2) ◽  
pp. 14 ◽  
Author(s):  
Divya Kaur ◽  
Xiuhong Cai ◽  
Umesh Khaniya ◽  
Yingying Zhang ◽  
Junjun Mao ◽  
...  

Photosystem II (PSII) uses water as the terminal electron donor, producing oxygen in the Mn4CaO5 oxygen evolving complex (OEC), while cytochrome c oxidase (CcO) reduces O2 to water in its heme–Cu binuclear center (BNC). Each protein is oriented in the membrane to add to the proton gradient. The OEC, which releases protons, is located near the P-side (positive, at low-pH) of the membrane. In contrast, the BNC is in the middle of CcO, so the protons needed for O2 reduction must be transferred from the N-side (negative, at high pH). In addition, CcO pumps protons from N- to P-side, coupled to the O2 reduction chemistry, to store additional energy. Thus, proton transfers are directly coupled to the OEC and BNC redox chemistry, as well as needed for CcO proton pumping. The simulations that study the changes in proton affinity of the redox active sites and the surrounding protein at different states of the reaction cycle, as well as the changes in hydration that modulate proton transfer paths, are described.


2005 ◽  
Vol 33 (5) ◽  
pp. 934-937 ◽  
Author(s):  
S. Yoshikawa

Bovine heart cytochrome c oxidase is a large multi-component membrane protein containing several phospholipids. X-ray structures of this enzyme at high resolution, determined recently, show a trigonal planar structure of CuB site in the O2 reduction site, which could contribute critically to the four-electron reduction of O2 bound at haem a3, and a hydrogen bond network, through which the proton pump is driven by haem a. The possible roles of phospholipids in the enzyme functions are discussed.


ACS Catalysis ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 8915-8924 ◽  
Author(s):  
Sohini Mukherjee ◽  
Manjistha Mukherjee ◽  
Arnab Mukherjee ◽  
Ambika Bhagi-Damodaran ◽  
Yi Lu ◽  
...  

2015 ◽  
Vol 44 (8) ◽  
pp. 1142-1144 ◽  
Author(s):  
Masahide Hikita ◽  
Akima Yamamoto ◽  
Kyoko Shinzawa-Itoh ◽  
Takashi Ogura ◽  
Shinya Yoshikawa

2010 ◽  
Vol 1797 ◽  
pp. 102-103 ◽  
Author(s):  
Kazumasa Muramoto ◽  
Kazuhiro Ohta ◽  
Kyoko Shinzawa-Itoh ◽  
Eiki Yamashita ◽  
Tomitake Tsukihara ◽  
...  

2009 ◽  
Vol 106 (7) ◽  
pp. 2165-2169 ◽  
Author(s):  
H. Aoyama ◽  
K. Muramoto ◽  
K. Shinzawa-Itoh ◽  
K. Hirata ◽  
E. Yamashita ◽  
...  

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