A cytochrome c oxidase proton pumping mechanism that excludes the O2 reduction site

FEBS Letters ◽  
2003 ◽  
Vol 555 (1) ◽  
pp. 8-12 ◽  
Author(s):  
Shinya Yoshikawa
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.


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

2011 ◽  
Vol 1807 (10) ◽  
pp. 1279-1286 ◽  
Author(s):  
Shinya Yoshikawa ◽  
Kazumasa Muramoto ◽  
Kyoko Shinzawa-Itoh

2015 ◽  
Vol 6 (1) ◽  
pp. 826-841 ◽  
Author(s):  
Puja Goyal ◽  
Shuo Yang ◽  
Qiang Cui

Understanding the mechanism of vectorial proton pumping in biomolecules requires establishing the microscopic basis for the regulation of both thermodynamic and kinetic features of the relevant proton transfer steps.


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