Interflavin oxidation-reduction reactions between pig kidney general acyl-CoA dehydrogenase and electron-transferring flavoprotein

Biochemistry ◽  
1985 ◽  
Vol 24 (24) ◽  
pp. 6830-6839 ◽  
Author(s):  
Robert J. Gorelick ◽  
Lawrence M. Schopfer ◽  
David P. Ballou ◽  
Vincent Massey ◽  
Colin Thorpe
1984 ◽  
Vol 224 (2) ◽  
pp. 577-580 ◽  
Author(s):  
M Madden ◽  
S M Lau ◽  
C Thorpe

Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins.


1994 ◽  
Vol 59 (3) ◽  
pp. 549-557
Author(s):  
František Skopal ◽  
Václav Dušek

Theoretical relationships and simplifying conditions have been derived for the feed of two reaction components into a nonisochoric reactor with ideal stirring. The feed of reaction components is controlled by the negative feedback at a constant absorbance of the reaction mixture. The theoretical relationships have been verified using model 2. order oxidation-reduction reactions of Ce(IV)/V(IV) and Fe(III)/V(III) in 1 M sulfuric acid at 20 °C.


1958 ◽  
Vol 19 ◽  
pp. 10-11 ◽  
Author(s):  
Balwant Singh ◽  
Sardul Singh

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