Stepwise Binding of Two Azide Ions to the O2-reduction Site of Bovine Heart Cytochrome c Oxidase Shown by Resonance Raman Analyses

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


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

Biochemistry ◽  
1993 ◽  
Vol 32 (27) ◽  
pp. 6923-6927 ◽  
Author(s):  
Stephen R. Lynch ◽  
Richard H. Carter ◽  
Robert A. Copeland

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