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. 2015 Jul 30;6:752. doi: 10.3389/fmicb.2015.00752

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.