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. Author manuscript; available in PMC: 2014 Nov 5.
Published in final edited form as: Biochim Biophys Acta. 2011 Nov 6;1817(4):506–517. doi: 10.1016/j.bbabio.2011.10.013

Table 1.

The calculated redox midpoint potentials (Em,7 at pH 7; in mV) of the redox-active cofactors for the different steps in the reaction cycle during the O to E transition in bovine CcO

Calculation/Experiment Transfer step Redox–active centers
CuA Fea Fea3 CuB
phase 1: [ET] 258a 270 150 0
140b 17[b]
phase 2: [PTpump/ET] 238 340 350 240
phase 3: [PTchem/ET] 267 380 355 490
phase 4: [pumping] 267 278 120 240

Exp.1:c pH 7.0 212–258 254–281 n.a.g 227–272
pH 7.0 224 267 n.a. 230
Exp.2:d pH 7.0 230–265 267–359 300–360 >400
Exp.3:e pH 7.0 270 342 330 n.a.
Exp.4:f pH 6.5 250 391 (238) 383 (405) 412
pH 8.0 250 359 (222) 350 (372) 366
a

The Em of the CuA center is adopted from ref. [89], see text for details.

b

The calculated Ems of heme a and heme a3 in phase 1, if residue E242 is in its deprotonated state.

c

Steady-state redox potential ranges of the metal centers in bovine CcO, taken from ref. [89], see also refs therein.

d

The range of Em values obtained from the equilibrium experiments performed in the anaerobic conditions or in the presence of an inhibitor (CO, CN, NO, etc.) in the BNC of bovine CcO, summarized from refs. [90, 93, 95, 97].

e

The Ems of the metal centers in bovine CcO obtained by fitting the experimental data to theoretical model. [55]

f

Experimental Ems of the redox centers, at pH 6.5 and 8.0, in CcO from P. denitrificans. For heme a and heme a3 are listed their high-asymptotic redox potentials. The numbers in brackets refer to the low-potential and high-potential heme transitions, see ref. [98] for details.

g

Data are not available.