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. Author manuscript; available in PMC: 2011 Aug 10.
Published in final edited form as: Biochemistry. 2010 Aug 10;49(31):6600–6616. doi: 10.1021/bi100407v

Table 3.

Kinetics data for the oxidative catalytic reaction of the different co-substrates: TCP, TBP and TFP with 0.5 μM DHP B and 150 μM of the corresponding co-substrates and varying H2O2 concentrations in 100 mM KPB pH 7

Co-Substrate DHP B
DHP A
Ratio c
kcatB/kcatA
KMH2O2
(μM)
KMTXP
(μM)
kcat
(s−1)
kcat/KMH2O2
(μM−1 s−1)
KMH2O2
(μM)
kcat
(s−1)
kcat/KMH2O2
(μM−1 s−1)



TFP a 96 ±
18
N/A N/A N/A 59 ±
10
N/A N/A 2.1
TCP a 22 ± 2 210 ±
23
1.53 ±
0.03
0.070 23 ± 1 0.61 ±
0.01
0.027 2.6
TCP b 35 ± 6 N/A 1.17 ±
0.05
0.034 16 ± 1 0.57 ±
0.01
0.036 2.1
TBP a 63 ±
15
315 ±
11
1.3 ± 0.1 0.021 11 ± 1 0.30 ±
0.01
0.027 4.3

N/A = not available

a

ferric starting oxidation state

b

oxyferrous starting oxidation state

c

as ratio of initial rate