Table 1.
Thermodynamic parameters for PpcA, PpcB, PpcD, and PpcE (Morgado et al., 2010a).
Cytochrome | Energy (meV) | |||
---|---|---|---|---|
Heme I | Heme III | Heme IV | Redox-Bohr center | |
PpcA | ||||
Heme I | −154 (5) | 27 (2) | 16 (3) | −32 (4) |
Heme III | −138 (5) | 41 (3) | −31 (4) | |
Heme IV | −125 (5) | −58 (4) | ||
Redox-Bohr center | 495 (8) | |||
PpcB | ||||
Heme I | −150 (3) | 17 (2) | 8 (2) | −16 (4) |
Heme III | −166 (3) | 32 (2) | −9 (4) | |
Heme IV | −125 (3) | −38 (4) | ||
Redox-Bohr center | 426 (8) | |||
PpcD | ||||
Heme I | −156 (6) | 46 (3) | 3 (4) | −28 (6) |
Heme III | −139 (6) | 14 (4) | −23 (6) | |
Heme IV | −149 (6) | −53 (6) | ||
Redox-Bohr center | 501 (8) | |||
PpcE | ||||
Heme I | −167 (4) | 27 (3) | 5 (3) | −12 (4) |
Heme III | −175 (4) | 22 (3) | 2 (4) | |
Heme IV | −116 (5) | −13 (4) | ||
Redox-Bohr center | 445 (10) |
All energies are reported in meV, with standard errors given in parentheses. For each cytochrome, the fully reduced and protonated protein was taken as reference. Diagonal values (in bold) correspond to oxidation energies of the hemes and deprotonating energy of the redox-Bohr center. Off-diagonal values are the redox (heme–heme) and redox-Bohr (heme–proton) interaction energies.