. Author manuscript; available in PMC: 2017 Jun 1.

Published in final edited form as: J Bioenerg Biomembr. 2016 Mar 1;48(3):325–333. doi: 10.1007/s10863-016-9655-y

Table 1.

Mutation^a	Deamino-NADH oxidase activity^b (nmoles/mg protein/min)	% Deamino-NADH oxidase activity^c
pBA400	165±48 (15)^c	100
K581C+R99C	160±12 (2)	97
pBA400-SpeI	95±8 (5)	100
T292+R99C	97±8 (2)	102

K581C+R99C was made in the background of pBA400, T292+R99C was made in the background of pBA400-SpeI

Activity was measured in membrane preparations as described in “Methods”. The mean, standard error and (number of measurements) are shown.

Activity is expressed as a percentage of the wild type rate.