Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 14, Problem 7P
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate ΔG for ATP hydrolysis at 37oC under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine
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Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP,calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate ∆G for ATP hydrolysis at 37 °C under these conditions.The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration.
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP.
a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85.
b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol)
The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )
The 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?
Chapter 14 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 14 - Prob. 1PCh. 14 - When pure reduced cytochrome c is added to...Ch. 14 - Freshly prepared mitochondria were incubated with...Ch. 14 - Prob. 4PCh. 14 - Prob. 5PCh. 14 - Prob. 6PCh. 14 - Intramitochondrial ATP concentrations are about 5...Ch. 14 - Prob. 8PCh. 14 - Prob. 9PCh. 14 - Years ago there was interest in using uncouplers...
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- Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP = creatine + ATP at 37 °C, as it occurs in the cytosol of neurons, where [phosphocreatine] = 4.7 mM, [creatine] = 1.0 mM, [ADP] = 0.73 mM, and [ATP] = 2.6 mM. Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds Phosphorylated compound AGʻ° (kJ/mol) phosphoenolpyruvate -61.9 phosphocreatine -43.0 ADP (→ AMP + P;) -32.8 ATP (→ ADP + P;) -30.5arrow_forward.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]arrow_forwardThe enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinatearrow_forward
- Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·molarrow_forwardThe ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.arrow_forwardCoupled reactions occur where a nonspontaneous reaction is enabled by coupling it to a spontaneous reaction. This approach is common in biological settings. Determine if ATP could be generated by this biochemical reaction. You have calculated that cell potential is +0.637V. An example of a coupled reaction is the first step of glycolysis, the phosphorylation of glucose to form glucose-6-phosphate shown below. kJ/mol The net AG° for this reaction is 1 2 3 н он H. H- H- H H H H 4 6. H. glucose phosphate anion glucose-6-phosphate AG = +14.0 kJ/mol 7 8 9. АТР ADP phosphate anion AG = -30.5 kJ/mol +/- LOarrow_forward
- a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?arrow_forwardThe protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.arrow_forwarda) (1) Calculate the physiological AG (not AG.) for the reaction: Phosphocreatine + ADP - creatine + ATP Given; Phosphocreatine + H;0 - creatine + Pi ADP + Pi → ATP + H;0 AG.' -43 kJ/mol AG.- +30.5 kJ/mol at 25°C as it occurs in the cytosol of neurons, in which phosphocreatine is present at 4.7 mM, creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM. (R = 8.315 JK-' mol-) (ii) Caleulate the free energy change at standard conditions for the following reaction: Acetaldehyde + NADH + H* + Ethanol + NAD* The half- reactions are: Acetaldehyde + 2H + 2e + Ethanol E°- - 0.20V NAD-+ 2H- + 2e ++ NADH + H- E=-0.32V (F= 96.485 kJ/V/mol)arrow_forward
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