scholarly journals Cytochrome c oxidase: Intermediates of the catalytic cycle and their energy-coupled interconversion

FEBS Letters ◽  
2011 ◽  
Vol 586 (5) ◽  
pp. 630-639 ◽  
Author(s):  
Alexander A. Konstantinov
2003 ◽  
Vol 101 (2) ◽  
pp. 529-533 ◽  
Author(s):  
D. Bloch ◽  
I. Belevich ◽  
A. Jasaitis ◽  
C. Ribacka ◽  
A. Puustinen ◽  
...  

FEBS Letters ◽  
1997 ◽  
Vol 412 (3) ◽  
pp. 405-409 ◽  
Author(s):  
T.V Vygodina ◽  
N Capitanio ◽  
S Papa ◽  
A.A Konstantinov

2008 ◽  
Vol 1777 ◽  
pp. S92
Author(s):  
Elena A. Gorbikova ◽  
Ilya Belevich ◽  
Mårten Wikström ◽  
Michael I. Verkhovsky

2000 ◽  
Vol 40 (supplement) ◽  
pp. S43
Author(s):  
E Yamashita ◽  
K. Hirata ◽  
T. Tsukihara ◽  
H. Aoyama ◽  
K. Muamoto ◽  
...  

1988 ◽  
Vol 550 (1 Cytochrome Ox) ◽  
pp. 161-166 ◽  
Author(s):  
PAOLO SARTI ◽  
GIOVANNI ANTONINI ◽  
RANCESCO MALATESTA ◽  
BEATRICE VALLONE ◽  
MAURIZIO BRUNORI

2016 ◽  
Vol 1857 ◽  
pp. e20
Author(s):  
Shinya Yoshikawa ◽  
Naomine Yano ◽  
Kazumasa Muramoto ◽  
Atsuhiro Shimada ◽  
Junpei Baba ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
F. Kolbe ◽  
S. Safarian ◽  
Ż. Piórek ◽  
S. Welsch ◽  
H. Müller ◽  
...  

AbstractCytochrome c oxidases are among the most important and fundamental enzymes of life. Integrated into membranes they use four electrons from cytochrome c molecules to reduce molecular oxygen (dioxygen) to water. Their catalytic cycle has been considered to start with the oxidized form. Subsequent electron transfers lead to the E-state, the R-state (which binds oxygen), the P-state (with an already split dioxygen bond), the F-state and the O-state again. Here, we determined structures of up to 1.9 Å resolution of these intermediates by single particle cryo-EM. Our results suggest that in the O-state the active site contains a peroxide dianion and in the P-state possibly an intact dioxygen molecule, the F-state may contain a superoxide anion. Thus, the enzyme’s catalytic cycle may have to be turned by 180 degrees.


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