Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Textbook Question
Chapter 18, Problem 16P
Energetics of the Hexokinase Reaction The standard-state free energy change.
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Standard redox potentials Eo' for some common compounds in biochemistry:
Eo' (Volt)
+ 0,81
+0,42
+ 0,25
12 O₂ + 2 H+ + 2 e
NO3 + 2 H+ + 2 e
2 cyt c (ox) + 2 e
2 cyt b (ox) + 2 e
Pyruvate + 2 H+ + 2 e*
NAD + 2 H+ + 2 e
Acétoacétate + 2 H+ + 2 e
(2) acétoacétate + NADH + H+
H₂O
NO₂ + H₂O
2 cyt c (red)
2 cyt b (red)
Lactate
(3) 2 cyt c (ox) + 2 cyt b (red)
NADH + H+
B-hydroxybutyrate
+ 0,08
- 0,19
With the help of the above table, determine the spontaneous direction of the following
reactions in the standard conditions. Justify your answers by calculating the Gibbs
(free) energy of reaction in each case.
(1) pyruvate + ß-hydroxybutyrate
-0,32
- 0,35
lactate + acétoacétate
B-hydroxybutyrate + NAD+
2 cyt c (red) + 2 cyt b (ox)
PRESSURE
OF A
WHAT IS THE asmoTIC
SOLUTION
OF BOVINE insuLIN (MOLAR MASS,
5700g mol - 1 ) aT
18 °C
IF 100.0 ML
OF
THE SOLUTION
conTains
0.103 a OF
THE INSULIN?
Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate
+ NADH Lactate + NADH+H+.
Note the temperature of this reaction will not affect the standard reducton potential delta E° in the table 13-7b.
Chapter 18 Solutions
Biochemistry
Ch. 18 - Characterizing Glycolysis List the reactions of...Ch. 18 - Radiotracer Labeling of Pyruvate from Glucose...Ch. 18 - Effects of Changing Metabolite Concentrations on...Ch. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - The Reactions and Meehanisms of the Leloir Pathway...Ch. 18 - The Effect of lodoacetic Acid on the...Ch. 18 - Prob. 8PCh. 18 - Comparing Glycolysis Entry Points for Sucrose...Ch. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Energetic of Fructose-1 ,6-bis P Hydrolysis...Ch. 18 - Prob. 15PCh. 18 - Energetics of the Hexokinase Reaction The...Ch. 18 - Prob. 17PCh. 18 - Distinguishing the Mechanisms of Class I and Class...Ch. 18 - Prob. 19PCh. 18 - Understanding the Mechanism of Hemolytic Anemia...Ch. 18 - Prob. 21PCh. 18 - Based on your residing of this chapter, what would...Ch. 18 - Examine the ActiveModel for alcohol dehydrogenase...Ch. 18 - Based on your knowledge of the structure of NAD+...Ch. 18 - Using the ActiveModel for phosphofructokinase...
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- Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.arrow_forwardBegining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potentialarrow_forwardTABLE 3-LACTATE PRODUCTION IN FORTIFIED HEMOLYSATES OF HUMAN ERYTHROCYTES* Substrate Glucose Glucose Lactate production† No. of experiments pH 6 7.1 2.03 ± 0.91 6 7.8 4.76 ± 1.09 7-1 10-73 +1-88 5 7.8 12.34 ±2.92 5 7.0 7-15±0.73 5 7-7 (b)( ) In mature erythrocytes (red blood cells) the end product of glycolysis is lactate because of the absence of mitochondria. On the right is a table comparing the rate of lac- tate production in hemolysates (lysed cells) of human RBCs as a function of pH with dif- ferent substrates introduced into the glyco- lytic pathway. The hemolysate was fortified with 30 μmoles substrate, 7.5 μmoles MgCl2, 10 μmoles disodium phosphate, 1.5 μmoles NAD and 5 μmoles ATP in a volume of 5 mL. The rate of lactate production is given as μmoles of lactate/g Hb/hr at 37° C, buffered to either pH 7.1 or 7.8, as indicated. According to the results in the table which glycolytic enzyme is rate-limiting? Explain. Glucose-6-phosphate Glucose-6-phosphate Fructose-1,6-diphosphate…arrow_forward
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH <=> Lactate + NADH+H+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b.arrow_forward6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?arrow_forwardBegining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.arrow_forward
- What is the Vmax of an enzyme at 1 μM with -4G RT k = 6.2x 10¹2 s-1 (Ideal gas constant R = 8.314 J K-1 mol-1) cat 0.14 μM S-1 1.4 µM s-1 14 μM s-1 0.14 mM s-1 1.4 mM s-1 activation energy (AG) of 55000 J/mol at 298K?arrow_forwardGiven that the reduction potential Eo'=-320, +10, +816, and +50mV for NAD+, fumarate, 02 and G3P DH bound FAD, respectively, calculate the free energy for a pair of electrons originating from the oxidation of glycerol-3-P to DHAP of, as it traverses the ETC. R = 8.315 x 10 J/mol K; Faraday constant, F= 96.48 KJ/V-mol, assume standard state T= 25°C and physiological conditions are T= 37°C. Report a whole number. Remember a Reduction potential is DEFINED as X(ax) +e- --> X(red) Be sure you have defined your oxidation and reduction species properly. kJ/molearrow_forwardThe molar absorption coefficient of cytochrome P450. an enzyme involved in the breakdown of harmful substances in the liver and small intestine. at 522 nm is 291 dm3 mol-1 cm-1. When light of that wavelength passes through a cell of length 6.5 mm containing a solution of the solute. 39.8 percent of the light was absorbed. What is the molar concentrat ion of the solute?arrow_forward
- calculate the actual free energy of hydrolysis of ATP, delta Gp in the erythrocytes of a new species. The standard free-energy of hydrolysis of ATP is also -30.5kJ/mol in this species, but the concentrations in this specie's erythrocytes are 0.00775 mM ATP, 0.00027 mM ADP and 0.00418 mM Pi. Assume the pH is 7.0 and the body temperature of this species is 43.0oC. Calculate your answer as kJ/mol to two decimal places.arrow_forwardEffects of Changing Metabolite Concentrations on Glycolysis In an erythrocyte undergoing glycolysis what would be the effect of a sudden increase in the concentration of a. AΤP? b. AMP? c. fructose-1.6-bisphosphate? d. fructose-2, 6-bisphosphate? e. citrate? f. glucose-6-phospthate?arrow_forwardDistinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.arrow_forward
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