Preparation and properties of soluble-insoluble nicotinamide coenzymes

1976 ◽  
Vol 18 (2) ◽  
pp. 199-208 ◽  
Author(s):  
Robert W. Coughlin ◽  
Masuo Aizawa ◽  
Marvin Charles
Keyword(s):  
Nicotinamide Coenzymes

THE 435 NM LEVEL IN REDUCED NICOTINAMIDE COENZYMES

1976 ◽  
Vol 24 (5) ◽  
pp. 473-474 ◽  
Author(s):  
Roberto Cadasei de Baptista ◽  
Adelaide Faljoni ◽  
Guiseppe Cilento
Keyword(s):  
Nicotinamide Coenzymes

scholarly journals Oxidation of nicotinamide coenzyme dimers by one-electron-accepting proteins

1986 ◽  
Vol 237 (3) ◽  
pp. 919-922 ◽  
Author(s):  
L Avigliano ◽  
V Carelli ◽  
A Casini ◽  
A Finazzi-Agrò ◽  
F Liberatore ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Cytochrome C ◽  
Electrochemical Reduction ◽  
Electron Acceptors ◽  
Single Electron ◽  
Redox Mechanism ◽  
Cytochrome C Reductase ◽  
Nicotinamide Coenzymes ◽  
Nadh Cytochrome ◽  
Phenazine Methosulphate

The nicotinamide nucleotide dimers (NAD)2 and (NADP)2, obtained by electrochemical reduction of NAD+ and NADP+, are able to reduce such single-electron acceptors as the proteins cytochrome c, azurin and methaemoglobin, though at different rates. Under the same conditions the reduced nicotinamide coenzymes NADH and NADPH are not able to reduce these proteins at measurable rates unless a catalyst (phenazine methosulphate or NADH-cytochrome c reductase in the case of cytochrome) is present. The redox mechanism seems to involve the formation of an NAD(P). radical that in the presence of O2 gives rise to superoxide (O2.-), since superoxide dismutase inhibited these reactions.

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