Table 3.
Redox potentials of Aβ-Cu(II) complex and common redox species of biological relevance.
System | E0’ (V vs NHE) |
---|---|
Norepinephrine | 0.384(1) |
Epinephrine | 0.372(1) |
Dopamine | 0.370(2) |
O2/H2O2 | 0.295(4) |
Cytochrome a | 0.290(1) |
Aβ-Cu(II) | 0.280 |
Cytochrome c | 0.250(1) |
Hemoglobin | 0.152(3) |
CoQ/CoQH2a | 0.100(1) |
Ascorbic acid | 0.051(3) |
Cytochrome b | 0.040(1) |
Fumarate/Succinate | 0.031(4) |
Myoglobin | 0.005(1) |
Crotonyl-CoA/Butyryl-CoA | −0.015(4) |
FMN/FMNH2b | −0.120(1) |
Oxaloacetate/malate | −0.166(4) |
Pyruvate/lactate | −0.185(4) |
Glutathione | −0.228(1) |
Vitamin B12 | −0.244(1) |
NAD+/NADHc | −0.320(1) |
FAD/FADH2d | −0.327(1) |
Coenzyme Q (ubiquinone) oxidized/reduced forms
Flavin mononucleotide oxidized/reduced forms
Nicotinamide adenine dinucleotide oxidized/reduced forms
Flavin adenine dinucleotide oxidized/reduced forms
G. Dryhurst, K. M. Kadish, F. Scheller, R. Renneberg, Biological Chemistry, Vol. 1, Academic Press, New York, London
D. C.-S. Tse, T. Kuwana, Anal. Chem., 50 (1978), 1315.
B. E. Conway, Electrochemical Data, Greenwood Press Publisher. New York
A. L. Lehninger, D. L. Nelson, M. M. Cox, Principles of Biochemistry, Worth Publishers. New York