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. Author manuscript; available in PMC: 2015 Jun 1.
Published in final edited form as: J Biol Inorg Chem. 2014 Mar 11;19(0):491–504. doi: 10.1007/s00775-014-1122-9

Table 1.

Steady-state kinetic parameters of HPCDs and MndDs.

Enzyme KMHPCA
(μM)
KMO2
(μM)
kcat/[metal]
(min−1)
kcat/KMHPCA
(μM−1 min−1)
kcat/KMO2
(μM−1 min−1)
Fe-HPCD 31 ± 6 60 470 ± 20 15 ± 2 7.8 ± 0.3
Mn-HPCD 35 ± 5 50 ± 4 370 ± 10 11 ± 2 7.4 ± 0.6
Co-HPCD 5 ± 1 1200 ± 100 215 ± 8a
590 ± 20b
1120 ± 70c
43 ± 9
120 ± 20
220 ± 50
0.18 ± 0.02
0.49 ± 0.05
0.9 ± 0.1
Mn-MndD 14 ± 4 62 360 ± 20 25 ± 4 5.8 ± 0.3
Fe-MndD 15 ± 4 37 ± 6 420 ± 20 28 ± 4 11.4 ± 1.4
a

Data from refs [8, 9, 13], measured under ambient O2 at 22 °C in 50 mM MOPS pH 7.8; unless otherwise noted.

b

measured in O2-saturated buffer at 22 °C.

c

Vmax extrapolated from Figure 3 of ref. [9].