Kinetic investigations of the reactions of cytochrome c oxidase with hydrogen peroxide

1986 ◽  
Vol 852 (1) ◽  
pp. 81-92 ◽  
Author(s):  
A.C.F. Gorren ◽  
H. Dekker ◽  
R. Wever
Biochemistry ◽  
1982 ◽  
Vol 21 (11) ◽  
pp. 2661-2666 ◽  
Author(s):  
David Bickar ◽  
Joseph Bonaventura ◽  
Celia Bonaventura

2009 ◽  
Vol 96 (3) ◽  
pp. 565a
Author(s):  
Michelle A. Yu ◽  
Gary J. Gerfen ◽  
Syun-Ru Yeh ◽  
Denis L. Rousseau

1983 ◽  
Vol 215 (2) ◽  
pp. 425-427 ◽  
Author(s):  
M Brunori ◽  
M C Silvestrini ◽  
M T Wilson ◽  
H Weiss

The reaction of Neurospora crassa cytochrome c oxidase with CO was studied by flash-photolysis and rapid-mixing experiments, leading to the determination of the association and dissociation rate constants (7 X 10(4) M-1 X s-1 and 0.02s-1 respectively). Pre-steady-state kinetic investigations of the catalytic properties of the enzyme showed that under proper conditions Neurospora cytochrome c oxidase can be ‘pulsed’, i.e. activated, like the mammalian enzyme. The ‘pulsed’ species is spectroscopically different from the ‘resting’ one, and the decay into the ‘resting’ state is fast (t1/2 approx. 3 min).


2010 ◽  
Vol 75 (11) ◽  
pp. 1352-1360 ◽  
Author(s):  
I. A. Bolshakov ◽  
T. V. Vygodina ◽  
R. Gennis ◽  
A. A. Karyakin ◽  
A. A. Konstantinov

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