Calculate the ΔG° for the making of 30 ATP from 30 ADP ATP + H2O ↔ ADP + Pi ∆G°’ = –30.5 kJ/mol ATP + H2O ↔ AMP + PPi ∆G°’ = –45.6 kJ/mol
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Calculate the ΔG° for the making of 30 ATP from 30 ADP
ATP + H2O ↔ ADP + Pi ∆G°’ = –30.5 kJ/mol
ATP + H2O ↔ AMP + PPi ∆G°’ = –45.6 kJ/mol
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- Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.Inside cells, the AG value for the hydrolysis of ATP to ADP + Pi is approximately -50 kJ/mol (-12 kcal/mol). Calculate the approximate ratio of [ATP] to [ADP][Pi ] in cells at 37°C. AG = AG + RT InKe R= 8.315 x 10³ kJ mol deg T= 298 K Table 15.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kJ mol- kcal mol- Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) -61.9 -14.8 -49.4 -11.8 -43.1 -10.3 -30.5 - 7.3 - 5.0 Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -20.9 -19.3 -4.6 -13.8 3.3 Glycerol 3-phosphate - 9.2 2.2 biochemistryWhat is the Vmax of an enzyme at 1 µM with an activation free energy (AG#) of 55000 J/mol at 298K? -AG # RT k cat = 6.2× 10¹² (Ideal gas constant R = 8.314 J K¯1 mol-¹1) 0.14 μM s-1 -1 S-1 1.4 μM s 14 μM s-1 0.14 mM s-1 1.4 mM s-1
- a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) aboveCalculate the actual, physiological ΔG for the reaction at 37 °C, as it occurs in the cytosol of neurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6 mM.In a living cell, this reaction is coupled with the hydrolysis of ATP. Symbolically, this reaction can be represented as ATP(aq) + H2O(l) → ADP(aq) + H2PO4−(aq) (ΔG° = −30.5 kJ/mol) Calculate ΔG° and K at 25°C for the following reaction. glutamic acid(aq) + ATP(aq) + NH3(aq) glutamine(aq) + ADP(aq) + H2PO4−(aq) find ΔG° in kJ and K
- a) (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)a) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) aboveAssume that the complete combustion of one mole of glucose to carbon dioxide and water liberates 2870 kJ/mol (AGo' = -2870 kJ/mol). If one contraction cycle in muscle requires 67 kJ, and the energy from the combustion of glucose is converted with an efficiency of 35% to contraction, how many contraction cycles could theoretically be fueled by the complete combustion of one mole of glucose? Round your answer to the nearest whole number. суycles per mole glucose
- 1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?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?What is the Keq for the conversion of Glucose 6-Phosphate to Glucose 1-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are -20.9 kJ/mol and -13.8 kJ/mol respectively? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 0.27 b 0.45 c 10.5 d 0.019 e 0.057 f 24.2 g 7.10 h 0.24 i 2477