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. Author manuscript; available in PMC: 2009 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2007 Nov 19;1777(1):32–38. doi: 10.1016/j.bbabio.2007.11.004

Table 1.

Rates of ATP Hydrolysis by Membrane Vesicles1

Mutation ATP hydrolysis2 (μmol/min/mg) + LDAO3 (fold increase4) + DCCD5 (% inhibition)
Wild type 0.9 3.9 (4.3) 80
R210Q/Q252R 0.25 3.2 (13) < 5
P204T/R210Q/Q252R 0.2 2.5 (12.7) < 5
R210Q/Q252K 0.5 2.4 (4.8) < 5
P204T/R210Q/Q252K 0.35 1.75 (5) < 5
R210Q 0.2 1.45 (7.2) 22
1

Rates shown are a typical set of values from three different experiments with similar results

2

ATP hydrolysis has been measured using phenol red as indicated in Materials and Methods.

3

ATP hydrolysis has been measured in the presence of 0.3% LDAO. Rates are given in μmol/min/mg.

4

The fold increase, shown in parentheses, is the ratio of the rate of ATP hydrolysis in the presence of 0.3% LDAO to the rate in the absence of LDAO.

5

Membrane vesicles were diluted 5-fold with buffer and incubated with 50 μM DCCD for 30 min at room temperature before assay, as described previously [20]. For the double and triple mutants it should be noted that the DCCD-inhibited rates were never significantly different from the similarly-treated controls.