name: 4. Electron transfer in the mitochondrial respiratory chain may be represented by the net reaction equation H20 + NAD* NADH + H* + 02 (a) Calculate AE'° for the net reaction of mitochondrial electron transfer. Use E'° values from Table 13-7. sinag Yn t noroest lierodT ITA did XNY) oalote dalipe A TAlo ano b Mt lln s (b) Calculate AG° for this reaction. -&.314 fodg ohnu iM (xMY) (c) How many ATP molecules can theoretically be generated by this reaction if the free energy of ATP synthesis under cellular conditions is 52 kJ/mol? ono l ban 9IA TTA TABLE 13-7b Standard Reduction Potentials of Some Biologically Important Half- Reactions Half-reaction E (V) Pyruvate+ 2H + 2e + lactate -0.185 Acetaldehyde + 2H* + 2e → ethanol FAD + 2H+ + 20 FADH2 -0.197 -0.219 Glutathione + 2H + 2e S+ 2H* + 2e+ H;S 2 reduced glutathione -0.23 -0.243 Lipoic acid + 2H* + 2e → dihydrolipoic acid -0.29 NAD* + H* + 2e NADH -0.320 NADP + H* + 2e + NADPH -0.324 Acetoacetate + 2H* + 2e > B-hydroxybutyrate a-Ketoglutarate + CO2 + 2H* + 2er + isocitrate 2H + 2e > H2 (at pH 7) Ferredoxin (Fe3*) + e> ferredoxin (Fe2") -0.346 4. -0.38 -0.414 -0.432 Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physical and Chemical Data, Vol. 1, p. 122, CRC Press, 1976. SThis is the value for free FAD; FAD bound to a specific flavoprotein (e.g. succinate dehydrogenase) has a ditferent E" that depends on its protein environment.

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4. Electron transfer in the mitochondrial respiratory chain may be represented by the net
reaction equation
H20 + NAD*
NADH + H* + 02
(a) Calculate AE'° for the net reaction of mitochondrial electron transfer. Use E'° values from Table
13-7.
sinag Yn
t noroest lierodT
ITA did
XNY) oalote
dalipe
A TAlo ano
b
Mt lln s
(b) Calculate AG° for this reaction.
-&.314
fodg ohnu iM
(xMY)
(c) How many ATP molecules can theoretically be generated by this reaction if the free energy of
ATP synthesis under cellular conditions is 52 kJ/mol?
ono l ban 9IA TTA
Transcribed Image Text:name: 4. Electron transfer in the mitochondrial respiratory chain may be represented by the net reaction equation H20 + NAD* NADH + H* + 02 (a) Calculate AE'° for the net reaction of mitochondrial electron transfer. Use E'° values from Table 13-7. sinag Yn t noroest lierodT ITA did XNY) oalote dalipe A TAlo ano b Mt lln s (b) Calculate AG° for this reaction. -&.314 fodg ohnu iM (xMY) (c) How many ATP molecules can theoretically be generated by this reaction if the free energy of ATP synthesis under cellular conditions is 52 kJ/mol? ono l ban 9IA TTA
TABLE 13-7b
Standard Reduction Potentials of Some Biologically Important Half-
Reactions
Half-reaction
E (V)
Pyruvate+ 2H + 2e + lactate
-0.185
Acetaldehyde + 2H* + 2e → ethanol
FAD + 2H+ + 20 FADH2
-0.197
-0.219
Glutathione + 2H + 2e
S+ 2H* + 2e+ H;S
2 reduced glutathione
-0.23
-0.243
Lipoic acid + 2H* + 2e → dihydrolipoic acid
-0.29
NAD* + H* + 2e
NADH
-0.320
NADP + H* + 2e + NADPH
-0.324
Acetoacetate + 2H* + 2e > B-hydroxybutyrate
a-Ketoglutarate + CO2 + 2H* + 2er + isocitrate
2H + 2e > H2 (at pH 7)
Ferredoxin (Fe3*) + e> ferredoxin (Fe2")
-0.346
4.
-0.38
-0.414
-0.432
Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physical
and Chemical Data, Vol. 1, p. 122, CRC Press, 1976.
SThis is the value for free FAD; FAD bound to a specific flavoprotein (e.g. succinate dehydrogenase) has a ditferent E" that depends
on its protein environment.
Transcribed Image Text:TABLE 13-7b Standard Reduction Potentials of Some Biologically Important Half- Reactions Half-reaction E (V) Pyruvate+ 2H + 2e + lactate -0.185 Acetaldehyde + 2H* + 2e → ethanol FAD + 2H+ + 20 FADH2 -0.197 -0.219 Glutathione + 2H + 2e S+ 2H* + 2e+ H;S 2 reduced glutathione -0.23 -0.243 Lipoic acid + 2H* + 2e → dihydrolipoic acid -0.29 NAD* + H* + 2e NADH -0.320 NADP + H* + 2e + NADPH -0.324 Acetoacetate + 2H* + 2e > B-hydroxybutyrate a-Ketoglutarate + CO2 + 2H* + 2er + isocitrate 2H + 2e > H2 (at pH 7) Ferredoxin (Fe3*) + e> ferredoxin (Fe2") -0.346 4. -0.38 -0.414 -0.432 Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physical and Chemical Data, Vol. 1, p. 122, CRC Press, 1976. SThis is the value for free FAD; FAD bound to a specific flavoprotein (e.g. succinate dehydrogenase) has a ditferent E" that depends on its protein environment.
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