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. 2014 May 14;9(5):e95391. doi: 10.1371/journal.pone.0095391

Table 3. Values of the second-order rate constant for peroxynitrite isomerization by ferric heme-proteins.

Heme-protein h app (M–1 s–1)
Methanosarcina acetivorans protoglobin* a 3.8×104
Mycobacterium tuberculosis truncated-hemoglobin N b 6.2×104
Pseudoalteromonas haloplanktis TAC125 truncated-hemoglobin O c 2.9×104
Horse heart myoglobin d 2.9×104
Sperm whale myoglobin e 1.6×104
Sperm whale myoglobin HisE7Ala mutant e 5.8×106
Sperm whale myoglobin HisE7Asp mutant e 4.8×106
Sperm whale myoglobin HisE7Leu mutant e 5.7×104
Sperm whale myoglobin PheCD1Trp/HisE7Leu mutant e 5.2×104
Sperm whale myoglobin HisE7Tyr/HisF8Gly mutant e 9.0×103
Human hemoglobin f 1.2×104
Human serum heme-albumin g 4.1×105
Cardiolipin-bound horse heart cytochrome c h 3.2×105
Carboxymethylated horse heart cytochrome c h 6.8×104
Cardiolipin-bound carboxymethylated horse heart cytochrome c h 5.3×105
a

pH 7.4 and 20°C. Present study.

b

pH 7.0 and 20°C. From [32].

c

pH 7.0 and 20°C. From [31].

d

pH 7.0 and 20°C. From [22].

e

pH 7.5 and 20°C. From [24].

f

pH 7.5 and 20°C. From [22].

g

pH 7.2 and 22°C. From [28].

h

pH 7.0 and 20°C. Cardiolipin was 1.6×10–4 M. From [29].