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. 2016 Feb 10;3(2):150379. doi: 10.1098/rsos.150379

Table 1.

Energetic consequences of catalytic activity determined according to the Rate Isotherm for a reaction proceeding at a fixed net rate of 10 mM s−1.

ATPase
ATP synthase
rf/rb rf (mM s−1) rb (mM s−1) ΔGdiss= RTln(rf/rb) (kJ mol−1) PMFa (mV) efficiency (%) PMFb (mV) efficiency (%)
1.01 1010 1000 0.026 155.38 99.95 155.54 99.95
1.1 110 100 0.246 154.70 99.51 156.23 99.51
11 11 1 6.177 136.25 87.65 174.67 89.00
101 10.1 0.1 11.889 118.50 76.22 192.43 80.79
103 10.01001 0.01001 17.795 100.13 64.41 210.79 73.75
104 10.001 0.001 23.727 81.69 52.55 229.24 67.82

aThe PMF in this column shows that generated from ATP hydrolysis (assuming a free energy gradient of ΔGATP=−50 kJ mol−1) in the face of the given free energy dissipation, ΔGdiss, determined according to the Rate Isotherm. It is calculated as PMF=(ΔGATPGdiss)/nF, where F is the Faraday constant and n=3.3˙H+/ATP. The corresponding thermodynamic efficiency is calculated as (ΔGATPGdiss)/ΔGATP. bThe PMF in this column is that required to synthesize ATP against its free energy gradient of 50 kJ mol−1 in the face of the given free energy dissipation, ΔGdiss, determined according to the Rate Isotherm. It is calculated as PMF=(ΔGATP−ΔGdiss)/nF. The corresponding thermodynamic efficiency is calculated as ΔGATP/(nF×PMF) or ΔGATP/(ΔGATP−ΔGdiss).