O2 binding properties of notable biological and synthetic examples.
| Compound | −ΔH (kJ mol−1) | −ΔS (J mol−1 K−1) | ΔG298 (kJ mol−1) | M–O2 assignment | Ref. |
|---|---|---|---|---|---|
| Fe(TpivPP)(1-MeIm)O2a | 65.3 | 183.0 | −10.8 | FeII–O2 | 55 |
| Co(TpivPP)(1-MeIm)O2a | 55.6 ± 3.8 | 192.5 ± 12 | 1.70 | CoIII–O2− | 62 |
| (Hemoglobin)O2b | 43.1 ± 4.6 | 74.1 ± 15.5 | −21.0 | FeII–O2/FeIII–O2− | 91 |
| (Hemoglobin)(O2)4c | 85.0 ± 18.0 | 190.6 ± 60.2 | −28.1 | FeII–O2/FeIII–O2− | 91 |
| [Cu2(N4PY2)(O2)]2+d | 58 ± 2 | 165 ± 8 | −9.0 | Cu2O22− | 64 |
| (Hemocyanin)O2e | 46 | 67 | −26 | Cu2O22− | 50 |
a
Collected in the solid state. 1-MeIm = N-methylimidazole.
b
Binding of the O2 to the first site in human hemoglobin in a buffer solution with pH = 7.6.
c
Binding of O2 to the fourth site human hemoglobin in a buffer solution with pH = 7.6.
d
N4 = N1N1N4N4-Tetrakis(2-(pyridin-4-yl)ethyl)butane-1,4-diamine.
e
Binding of O2 to P interruptus hemocyanin in buffer solution with pH = 9.6.