Intramitochondrial ATP concentrations are about 5 mM, and phos-phate concentration is about 10 mM. If ADP is five times moreabundant than AMP, calculate the molar concentrations of ADP andAMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at37 °C under these conditions. The energy charge is the concentra-tion of ATP plus half the concentration of ADP divided by the totaladenine nucleotide concentration:[ATP] + 1/2[ADP][ATP] + [ADP] + [AMP]

ATP (Adenosine triphosphate) is the energy stored in the body which is produces as the result of…

Answered: Intramitochondrial ATP concentrations…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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] )
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;) -30.5
The 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.
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?
The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]
The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1
If a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.
Given the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin at 25oC: ΔH° = –88 kJ/mol ΔS° = 0.3 kJ/mol. The free energy of hydrolysis of ATP in systems free of Mg2+ is −35.7 kJ/mol. When the concentration of this ion is 5 mM, ΔG°observed is approximately −31 kJ/mol at pH 7 and 38°C. Suggest a possible reason for this effect.
The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
Calculate the standard free energy for creatine-phosphate hydrolysis in a cell where [creatine-P]=3 mM, [creatine]=2 mM, and [Pi]= 12.1 mM. Is the reaction exergonic or endogonic?
The isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is catalyzed by triose phosphate isomerase. In the cell, the concentration ratio of DHAP/GAP = 5.5. Calculate [DHAP] (in M) when [GAP] = 0.00002

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