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. Author manuscript; available in PMC: 2016 Sep 1.
Published in final edited form as: Free Radic Biol Med. 2015 May 28;86:308–321. doi: 10.1016/j.freeradbiomed.2015.05.018

Table 3. The reduction potential E1/2 vs NHE, kcat(H2O2) for the catalysis of H2O2 dismutation and log kcat(O2.−) for the catalysis of O2.− dismutation of various redox-active compounds and catalase.

If not indicated, the data are taken from [19, 21, 22, 49, 50]. The catalysis of H2O2 dismutation was followed in 0.05 M tris buffer at (25±1) °C with Clark oxygen electrode. In case of Fe(III) porphyrins, Mn(III) salen and Mn(II) cyclic polyamines the E1/2 relates to the MIII/MII redox couple, while it relates to MIV/MIII redox couple in case of Fe(III) corrole. The catalysis of O2.− dismutation was followed in 0.05 M potassium phosphate buffer, pH 7.8 at (25±1) °C as described in references [49, 50, 83]. The kcat(H2O2) value for Fe corrole was determined at 37 °C [53], while kcat(O2.−) was measured at (25±1) °C [52].

Compound E1/2, mV vs NHE kcat (H2O2), M−1 s−1 log kcat (O2.−)
FeTE-2-PyP5+, a +211 803.5 8.05
FeTnOct-2-PyP5+, a +261 368.4 7.09
FeTrF5Ph-β(SO3)2-corrole2− +1050b 6400c 6.48d
MnCl2 +850e none 6.11–6.95
Mn Salen, EUK-8 +130 13.5 6.36f
M40403 +525(ACN) 8.2 7.08
M40404 +452(ACN) 6.5 none
Nitroxide, Tempol +810g none < 3 at pH 7.8
Nitrone, NXY-059 none
Ebselen none
Catalase enzyme 1.5 × 106
a

At physiological pH the FeTE(or nOct)-2-PyP5+ has one hydroxo ligand bound axially and thus carries 4+ total charge;

b

refs [19, 21];

c

the kcat(H2O2) was determined at 37°C [53];

d

ref [52];

e

oxidation potential only;

f

corrected value;

g

one-electron reduction potential relates to RNO+/RNO redox couple.