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TABLE 13-7 Standard Reduction Potentials of Some Biologically Important Half Half-reaction Ero (V) 0.816 0.421 NO 2H + 2e >NO H20 Cytochrome f(Fcytochromef Fe) 0.365 Fe(CN) (ferricyanide) +eFe(CN)6 0.36 Cytochrome a3 (Fecytochrome az (Fe*>) 035 0.295 Cytochrome a (Fe3 +cytochrome a (F 0.29 Cytochrome c Fcytochrome c (Fe) 0254 Cytochrome cl (Fe3-ㄧ˙-cytochrome cl (Fe2+) 0.22 Cytochrome (Fecytochrome (Fe 0.077 Ubiquinone 2H 2eubiquinol Fumarate+2H+2esuccinate2 2Ht+2e-H2 (at standard conditions, pH0)0.000 Crotonyl-CoA 2H 2e butyryl-CoA Oxaloacetate+2Ht+2e- malate Pyruvate+ 2H 2elactate Acetaldehyde 2H+2e-ethanol FAD 2H2eFADH2 Glutathione-2 Г-2e--2 reduced glutathione -0.23 0.045 0.031 -0.015 -0.166 -0.185 -0.197 -0.2192 -0.243 -0.29 -0.320 -0.324 Lipoic acid-2H-2e-→ dihydrolipoic acid NADPH2eNADPH Acetoacetate 2H2eB-aydroxybutyrate 0.346 a-Ketoglutarate+ CO2-2H-2e-→ isocitrate -0.38 2r-2e-→H2 (at pH 7) Ferredoxin (Fe5+) + e-→ferredoxin (Fe2+) -0.432 Source: Data mostlv from R A Loach. in Hanabook of Biochemistry and olecular Biolog (G. D. Fasman, ed.), Plysical and Chemical Data, Vol. 1, p. 122, CRC Press, 1976. -0.414 3rd edn This is the value for free FAD: FAD bound to a specific flavoprotein (e.g, succinate dehydrogenase) has a different E that depends on its protein environment.

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-0 29 0 71 0.24 to .045 0335y m(D)、

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