Spectroscopic and rapid kinetic studies of complex formation and electron transfer between hydroxylamine oxido-reductase and cytochrome c-554 from Nitrosomonas europaea

1989 ◽  
Vol 36 (3-4) ◽  
pp. 217 ◽  
Author(s):  
D.M. Arciero ◽  
C. Balny ◽  
A.B. Hooper
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Complex Formation ◽  
Kinetic Studies ◽  
Nitrosomonas Europaea

scholarly journals Efficient Encounter Complex Formation and Electron Transfer to Cytochrome  c Peroxidase with an Additional, Distant Electrostatic Binding Site

2020 ◽  
Vol 59 (51) ◽  
pp. 23239-23243
Author(s):  
Antonella Di Savino ◽  
Johannes M. Foerster ◽  
Thijmen La Haye ◽  
Anneloes Blok ◽  
Monika Timmer ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Complex Formation ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Encounter Complex ◽  
Electrostatic Binding

scholarly journals Efficient Encounter Complex Formation and Electron Transfer to Cytochrome  c Peroxidase with an Additional, Distant Electrostatic Binding Site

2020 ◽  
Vol 132 (51) ◽  
pp. 23439-23443
Author(s):  
Antonella Di Savino ◽  
Johannes M. Foerster ◽  
Thijmen La Haye ◽  
Anneloes Blok ◽  
Monika Timmer ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Complex Formation ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Encounter Complex ◽  
Electrostatic Binding

scholarly journals Electron transfer between soluble and immobilized mammalian cytochrome c. Equilibrium and kinetic studies on immobilized cytochrome c

1976 ◽  
Vol 153 (3) ◽  
pp. 657-661 ◽  
Author(s):  
A Colosimo ◽  
M Brunori ◽  
E Antonini
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Kinetic Studies ◽  
Reduced Form ◽  
Experimental Conditions ◽  
Horse Heart Cytochrome ◽  
Ferrocytochrome C ◽  
Matrix Bound ◽  
Semi Solid

Horse heart cytochrome c was covalently bound to Sepharose 4B and its redox properties were measured under various experimental conditions. The equilibrium constant for the electron exchange between the oxidized and the reduced form of cytochrome c when one of the two forms was in the semi-solid state and the other one in solution was close to 1. Matrix-bound ferrocytochrome c is very stable to autoxidation and is not oxidized by O2 even in the presence of mammalian cytochrome oxidase. Oxidation occurs if catalytic amounts of soluble cytochrome c are added to the reaction mixture. The rate of oxidation of matrix-bound ferrocytochrome c in the presence of cytochrome oxidase and catalytic amounts of soluble cytochrome c may be correlated with the rate of electron transfer between soluble and matrix-bound cytochrome c. This rate is more than two orders of magnitude lower than that reported for the homonuclear (between identical species) electron transfer in solution.

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