If palmitic acid is subjected to complete combustion in a bomb calorimeter,one can calculate a standard free energy of combustion of 9788 kJ/mol.From the ATP yield of palmitate oxidation, what is the metabolic efficiencyof the biological oxidation, in terms of kilojoules saved as ATP per kilojoulereleased? (Ignore the cost of fatty acid activation.)

Palmitic acid is a saturated long-chain fatty acid with a 16-carbon backbone. It is found naturally…

Answered: If palmitic acid is subjected to…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

Consider the fructose-1,6-bisphosphatase reaction. Calculate the free energy change if the ratio of the concentrations of the products to the concentrations of the reactants is 21.7 and the temperature is 37.0°C? AG' for the reaction is -16.7 kJ/mol. AG = kJ/mol
During electron transfer through the mitochondrial respiratory chain, the overall reaction is NADH + 1/2O2 + H+ arrow forward NAD+ + H2O. The difference in reduction potentials for the two half reactions (delta E) is +1.14 V. Show how you would calculate the standard free energy change, delta G, for the reaction as written. (faraday constant is 96.48 kj/vmol: R=8.314j/mol K=1.987 cal/mol K
In a major metabolic pathway involving the monosaccharide glucose, one of the reactions involve the conversion of glucose to glucose-6-phosphate summarized below together with accompanying free energy change: glucose + phosphate = glucose-6-phosphate + H,0 AG = 13.8 kJ · mol-1 (Reaction 1) In cells, the production of G6P (Reaction 1 above) is coupled to a reaction that involves the hydrolysis of ATP to ADP (shown below, Reaction 2) which makes the overall reaction much more favorable to the production of glucose-6-phosphate. ATP + H,O = ADP + phosphate (Reaction 2) Why do you think coupling the production of glucose-6-phosphate to the hydrolysis of ATP makes the overall reaction spontaneous? What can you say about the free energy change accompanying the hydrolysis of ATP (Reaction 2)?
For part (b) of this problem, use the following standard reduction potentials, free energies, and nonequilibrium concentrations of reactants and products: Consider the last two steps in the alcoholic fermentation of glucose by brewer’s yeast: pyruvate + NADH + 2H+ → ethanol + NAD+ + CO2 (a) Do you predict that ∆S° for this reaction is > 0 or < 0? (b) Calculate the nonequilibrium concentration of ethanol in yeast cells, if ∆G = -38.3 kJ/mol for this reaction at pH = 7.4 and 37 °C when the reactants and products are at the concentrations given above. (c) How would a drop in pH affect ∆G for the reaction described in part (b)? (d) How would an increase in intracellular CO2 levels affect ∆G for the reaction in part (b)? (e) How would an increase in intracellular CO2 levels affect ∆G°′ for the reaction in part (b)?
Calculate the equilibrium concentration of H2O for the following esterification reaction performed in ethanol(C2H5OH) C2H5OH + CH3CO2H ⇌CH3CO2C2H5 + H2O KC= 4.0 At equilibrium: [CH3CO2H] = 0.75 M; [CH3CO2C2H5 ]= 2.2 M
Given what you know about the involvement of nicotinamide nucleotides in oxidative and reductive metabolic reactions, predict whether the following intracellular concentration ratios should be (1) unity, (2) greater than unity, or (3) less than unity. Explain your answers. (a) [NAD*]/[NADH] (b) [NADP*]/[NADPH] Because NAD* and NADP* are essentially equivalent in their ten- dency to attract electrons, discuss how the two concentration ratios might be maintained inside cells at greatly differing values.
The maximum saturation, 28.3ug of enzyme in 25ml water catalyzes the oxidation of ethanol at a rate of 2.5mm/min. Calculate the kcat in units of seconds if the enzyme has a molar mass of 65kg/mol.
The phosphorylation and oxidative decarboxylation of oxaloacetate by inorganic phosphate (Pi) to make phosphoenolpyruvate and carbon dioxide is endergonic under intracellular conditions. It is characterized by this equation: Oxaloacetate + Pi ←→ Phosphoenolpyruvate + H2O + CO2 ΔG’ = +24.6 kJ/mol The synthesis of GTP from GDP and inorganic phosphate (Pi) in solution is endergonic under intracellular conditions, and it is characterized by this equation: GDP + Pi ←→ GTP + H2O ΔG’ = +30.5 kJ/mol Write a new net thermodynamically coupled reaction equation that describes the synthesis of phosphoenolpyruvate from oxaloacetate using the hydrolysis of GTP to power the reaction and calculate the new net ΔG’ of this reaction. Show all of your work.
Standard Reduction Potentials of Some Biologically Important Half- Reactions Half-reaction E" (V) Pyruvate- + 2H + 2e → lactate- -0.185 Acetaldehyde + 2H* + 2e- → ethanol -0.197 FAD + 2H+ + 2e → FADH2 -0.219a Glutathione + 2H* + 2e- → 2 reduced glutathione -0.23 S+ 2H* + 2e → H2S -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 -0.346 a-Ketoglutarate + CO2 + 2H* + 2e- → isocitrate -0.38 2H* + 2e- > H2 (at pH 7) --0.414 Ferredoxin (Fe3+) + e- → ferredoxin (Fe2+) -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. 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.
Free energy changes under intracellular conditions differ markedly from those determined under standard conditions. AG" =-30.5 kJ/mol for ATP hydrolysis to ADP and P,. Calculate AG for ATP hydrolysis in a cell at 37 °C that contains [ATP] =3 mM, [ADP] =1mM, and [P] =1 mM.
The reaction below occurs in nearly all human cells. It is catalyzed by the enzyme enolase. CO- CO- enolase -OPO3 OPO3 + H20 ČH,OH AGO'=+1.7 kJ/mol CH2 2PGA PEP Under cellular conditions, the AG is -3.3 kJ/mol. Which of the following could account for these changes in cellular AG compared to the standard biological free energy? The concentration of 2PGA is 7 times higher than PEP. The concentration of PEP is 7 times higher than 2PGA Enolase lowers the activation energy of the transition state. The release of water from 2PGA is a form of energy coupling.
Compare the metabolic efficiencies of complete oxidation of fat (use 1,2-stearoyl-3-palmitoleoyl-glycerol as your example!) versus glucose in terms of moles of NADH equivalents (e.g., FADH2 and NADH) per gram (assume that all of the compounds of interest are in their anhydrous form) electron equivalents per gram O2 consumed per gram.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS