60. The standard free energy change (ΔG°′) for ATP hydrolysis is −30 kJ·mole−1. The in vivo concentrations of ATP, ADP and Pi in E. coli are 7.90, 1.04 and 7.90 mM, respectively. When E. coli cells are cultured at 37 °C, the free energy change (ΔG) for ATP hydrolysis in vivo is __________ kJ·mole−1.

60. The standard free energy change (ΔG°′) for ATP hydrolysis is

−30 kJ·mole−1. The in vivo concentrations of ATP, ADP and
Pi in E. coli are 7.90, 1.04 and 7.90 mM, respectively.
When E. coli cells are cultured at 37 °C, the free energy
change (ΔG) for ATP hydrolysis in vivo is
__________ kJ·mole−1.

 

The free energy change (ΔG) for ATP hydrolysis in vivo in E. coli cells cultured at 37°C is -47.7 kJ·mol-1, more negative than the standard value due to non-equilibrium concentrations.

Calculation Method

ATP hydrolysis follows ATP + H2O → ADP + Pi, with ΔG = ΔG°′ + RT ln Q, where Q = [ADP][Pi]/[ATP].

Concentrations convert to 0.00790 M ATP, 0.00104 M ADP, and 0.00790 M Pi, yielding Q = 0.00104.

At T = 310 K (37°C), R = 0.008314 kJ·mol-1·K-1, RT ln Q ≈ -17.7 kJ·mol-1, so ΔG = -30 + (-17.7) = -47.7 kJ·mol-1.

Biochemical Significance

In vivo, ΔG becomes more exergonic than ΔG°′ = -30 kJ·mol-1 because low Q (far below equilibrium K ≈ 105–106) drives energy release for cellular work.

E. coli maintains high ATP/ADP ratios via metabolism, enhancing ATP’s utility in biosynthesis and transport.

Common Options Explained

Typical multiple-choice options test formula application or unit errors:

Option Value (kJ·mol-1) Reason Incorrect
-30.0 Matches ΔG°′ Ignores actual concentrations
-35.0 to -40.0 Approximate errors Wrong T (e.g., 298 K) or R
-47.7 Correct Uses 310 K, mM-to-M conversion
-50.0+ Overestimation Faulty ln Q or units

This precise value underscores physiological thermodynamics in microbiology.

 

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