2+ The binding constant for the Mg²+ ion to ATP is about (0.1 mM)¹. How much energy is required to detach a magnesium ion from ATP at standard conditions?
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- As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG°) of ATP = -31 kJ/mol; RT = 2.58 kJ/mol) %3D %3D Select one: a. -33 kJ/mol b. -28 kJ/mol C. -19 kJ/mol d. -42 kJ/molCalculate 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 AG = Phosphorylated compound phosphoenolpyruvate phosphocreatine ADP (→ ATP (→ AMP + P;) ADP + P₁) AG' (kJ/mol) -61.9 -43.0 -32.8 -30.5 kJ/mol. (a) Calculate the standard free energy change as a pair of electrons is transferred from succinate to molecular oxygen in the mitochondr- ial respiratory chain. (b) Based on your answer in part (a), calculate the maximum num- ber of protons that could be pumped out of the matrix into the intermembrane space as these electrons are passed to oxygen. Assume 25 °C, ApH = 1.4; A = 0.175 V (matrix negative). (c) At which site(s) are these protons pumped?
- 7. Using the AG" for the hydrolysis of ATP, calculate the AG for the hydrolysis of ATP in erythrocytes (red blood cells). The normal cytosolicconcentrations of ATP, ADP and Pi are 2.0, 0.2 and 1mM, respectively.Calculate the equilibrium constant at 37oC for the reactionGlucose + 6O2 + 36ADP + 36Phospate → 6CO2+ 42H2O +36ATP ... ... ...Gibbs free energychange of Go= − 423 kcal/mole of GlucoseCalcium ions bind to a Ca2+-ATPase which has two identical calcium sites, in two stages with apparent equilibrium constants of K, = 3.5 x 105 and K2 = 2 x 106. Determinet for this binding.
- . The following data describe the binding of oxygen to human myo- globin at 37 °C. Po, (mm Hg) Ро, (mm Hg) Yo, Yoz 0.5 0.161 0.697 1 0.277 8 0.754 2 0.434 12 0.821 3 0.535 20 0.885 4 0.605 From these data, estimate (a) Pg9 and (b) the fraction saturation of myoglobin at 30 mm Hg, the partial pressure of O, in venous blood. . What qualitative effect would you expect each of the following to have on the P50 of hemoglobin? (a) Increase in pH from 7.2 to 7.4 (b) Increase in Pco, from 20 to 40 mm Hg (c) Dissociation into monomer polypeptide chains(b) Hydrazine (N,H4) is used for rocket fuel. Calculate the percentage atom' economy for hydrazine production 2NH3 +NaOC1→ N„H4 +NaCl +H2O (c) How is ultrasound employed to energize chemical reactions?Glycolysis is the process by which glucose is metabolized to lactic acid according to the equation C6H12O6(aq)2C3H6O3(aq) G=198 kJ at pH 7.0 and 25°C Glycolysis is the source of energy in human red blood cells. In these cells, the concentration of glucose is 5.0103 M, while that of lactic acid is 2.9103 M. Calculate AG for glycolysis in human blood cells under these conditions. Use the equation G=G+RT In Q, where Q is the concentration quotient, analogous to K.
- A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction HAPPY ⇌ SAD. The researchers begin to characterize the enzyme. (a) In the first experiment, with [Et] at 4 nM, they find that the Vmax is 1.6 μM s−1. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) (b) In another experiment, with [Et] at 1 nM and [HAPPY] at 30 μM, the researchers find that V0 = 300 nM s−1. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) (c) Further research shows that the purified happyase used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase preparation and the two experiments repeated, the measured Vmax in (a) is increased to 4.8 μM s−1, and the measured Km in (b) is now 15 μM. For the inhibitor ANGER, calculate the values of α and α′. . (d) Based on the information given…Describe the energetics of the given reactions: a) 1/₂+1/20+90.29 kJ-NO b) Pb +S+20, PbS0+9918.39 kJThe degradation of the antibiotic clindamycin stored at 343 K in aqueous solution at pH 4 is found to be first order with a rate constant of 2.49 x 10−7 s −1. Over the temperature range 320 K to 360 K theactivation energy was found to be 123.3 kJ mol−1. (a) Calculate the rate constant at 325 K.(b) The threshold for product safety is 1% degradation. At 295 K the time taken for 1% of the antibiotic to degrade is found to be close to 0.01/ k. Comment on the shelf-life of the drug.