To review:
The value of
Introduction:
In living cells, the concentration of ATP and the product of hydrolysis of ATP (ADP and Pi) islower than that of the standard 1 M concentrations. This is the reason why the actual free energy of ATP hydrolysis differs from the standard free energy. So, it is difficult to obtain an accurate measure of the concentrations of cellular components.
Explanation of Solution
As per the given data, the actual
Using the values, as given in the statement. The equation becomes:
The values of ATP, ADP, and Pi are given in mM. So, to covert, these values in M divide each value by 1000. The resulting values obtained would be: 0.004, 0.00135, and 0.00465 for ATP. ADP, and Pi, respectively. Here, R is the gas constant and its value is 8.134 j/mol. The temperature was given in Celsius and has been converted into kelvin for calculation. (
From the above calculation, the actual
Thus, it can be concluded that at a certain concentration of ATP, the actual value of
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Chapter 4 Solutions
Biochemistry: The Molecular Basis of Life
- If the Go for ATP hydrolysis into ADP + inorganic phosphate is 7.3 kcal/mole, and the Go for glutamine synthesis from glutamic acid and NH3 is +3.4 kcal/mole, calculate the average Go for coupling these two reactions (glutamic acid + NH3 + ATP glutamine + ADP + inorganic phosphatearrow_forwardIf a slight deficiency in the Vitamin B1 derivative Thiamine Pyrophosphate (TPP) leads to an accumulation of substrates for reactions utilizing this cofactor, A) what substrates would ‘accumulate’ in a human after eating a an enormous amount of sugar-laden Halloween candy, AND what would be the regulatory consequences on carbohydrate metabolism? B) what substrates would accumulate in yeast cells cultured under anaerobic (no oxygen) conditions AND what would be the regulatory consequences on carbohydrate metabolism? C) and lastly, what substrates would accumulate in plant cells incorporating carbon and generating energy solely using photosynthesis?arrow_forwardIf a slight deficiency in the Vitamin B1 derivative Thiamine Pyrophosphate (TPP) leads to an accumulation of substrates for reactions utilizing this cofactor, A) what substrates would ‘accumulate’ in a human after eating a an enormous amount of sugar-laden Halloween candy, AND what would be the regulatory consequences on carbohydrate metabolism? B) What substrates would accumulate in yeast cells cultured under anaerobic (no oxygen) conditions AND what would be the regulatory consequences on carbohydrate metabolism? C) What substrates would accumulate in plant cells incorporating carbon and generating energy solely using photosynthesis?arrow_forward
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- Assume that you have a solution of 0.1 M glucose 6-phosphate. To this solution you add the enzyme phosphoglucomutase, which catalyzes the reaction: glucose-6-P ⇔ glucose-1-P ∆G°′ = +1.7 kJ/mol (a) Does this reaction proceed at all as written at 25 °C, and if so, what are the final concentrations of glucose 6-P and glucose 1-P? (b) What effect would omitting the enzyme have on the reaction. Be specific. (c) Under what cellular conditions, if any, would this reaction continuously produce glucose 1-P at a high rate?arrow_forwardWhat terms would best describe the above coupled reaction? (If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for maltose synthesis from glucose + glucose is +3.7 kcal/mole, calculate the standard free energy change for the combined reaction of ATP + glucose + glucose g ADP + maltose + inorganic phosphate.) it is non-spontaneous and endothermic (because the overall DGo is negative) it is spontaneous and exothermic (because the overall DGo is negative) it is non-spontaneous and endothermic (because the overall DGo is positive) it is spontaneous and exothermic (because the overall DGo is positive) it is non-spontaneous and exothermic (because the overall DGo is negative)arrow_forwardThe formation of glutamine from glutamate and ammonium ions requires 14.2 kJ mol-1 of energy input. It is driven by the hydrolysis of ATP to ADP mediated by the enzyme glutamine synthetase. {a) Given that the change in Gibbs energy for the hydrolysis of ATP corresponds to ΔG = -31 kJ mol-1, under the conditions prevailing in a typical cell , can the hydrolysis drive the formation of glutamine? (b) What amount {in moles) of ATP must be hydrolysed to form 1 mol glutamine? (c) Suppose that the radius of a typical cell is 10 μm and that inside it 106 ATP molecules are hydrolysed each second. What is the power density of the cell in watts per cubic metre (1W = 1 Js- 1)? (d) A computer battery delivers about 15 Wand has a volume of 100 cm3 Which has the greater power density, the biological cell or the battery?arrow_forward
- Based on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surelyarrow_forwardThe standard free energy variation of the ATP hydrolysis reaction is ΔGº’ = -30.5 kJ / mol ATP + H2O ⇄ ADP + Pi In red blood cells, when the concentration of Pi is 1.6 mM, the real change in energy free is ΔG = - 50'2 kJ / mol. a) Calculate under these conditions what is the ratio [ATP] / [ADP] in the red blood cells. b) Determine the equilibrium constant K 'of the reaction outlined above. c) If the ADP concentration were 0.2mM, what would be the effective concentration of ATP corresponding to equilibrium.arrow_forwardConsider the following chemical reaction: Glucose + ATP → Glucose-6-Phosphate + ADP + Pi Given the following information, calculate the actual free energy change (G’) of this reaction. G’ of Glucose + ATP → Glucose-6-Phosphate + ADP + Pi = -16.7 kJ/mol [Glucose] = 5.0 mM [ATP] = 1.85 mM [Glucose-6-Phosphate] = 0.083 mM [ADP] = 0.14 mM [Pi] = 1.0 mM Temperature = 37 C R (Gas Constant) = 8.314 J/mol•Karrow_forward
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