O2 Reduction by Biosynthetic Models of Cytochrome c Oxidase: Insights into Role of Proton Transfer Residues from Perturbed Active Sites Models of CcO

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


2001 ◽  
Vol 98 (9) ◽  
pp. 5013-5018 ◽  
Author(s):  
M. Branden ◽  
H. Sigurdson ◽  
A. Namslauer ◽  
R. B. Gennis ◽  
P. Adelroth ◽  
...  

2015 ◽  
Vol 1847 (8) ◽  
pp. 690-697 ◽  
Author(s):  
Vivek Sharma ◽  
Pauliina Ala-Vannesluoma ◽  
Ilpo Vattulainen ◽  
Mårten Wikström ◽  
Tomasz Róg

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