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. Author manuscript; available in PMC: 2015 May 6.
Published in final edited form as: Bioorg Med Chem Lett. 2008 Nov 24;19(3):972–975. doi: 10.1016/j.bmcl.2008.11.071

Table 1.

Kinetic properties of purified pfNDH2 in the presence of electron-accepting substrates

Electron acceptor kcat (1/min)a Kma,b
CoQ0 20.0 ± 0.3 104.3 ± 6.6
CoQ1 0.9 ± 0.1 2.2 ± 1.2
CoQ4 n.a. n.a.
CoQD n.a. n.a.
Menadione 4.6 ± 0.2 239.3 ± 22.4
DCIP 1.9 ± 0.0 4.6 ± 0.4
a

Km and kcat values and standard deviations were calculated from three independent experiments. n.a., enzyme activity not observed.

b

For each Km determination, the concentration of either the electron acceptor or NADH was varied while the other substrate was fixed at 500 µM. Km and kcat values were determined using best-fit Michaelis–Menton curves.