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

Published in final edited form as: FEBS J. 2016 Nov 18;283(24):4491–4501. doi: 10.1111/febs.13933

Table 2. Fate of the H₄B radical following its formation in the Arg hydroxylation reaction.

The percentage of oxidized (H₂B) or reduced (H₄B) cofactor that was present in each NOS enzyme at the end of their Arg hydroxylation reaction was determined. Values represent the mean ± S.D. of at least three independent measurements of each enzyme. WT, wild-type.

Enzyme	Conditions	% of H₄B	% of H₂B
WT nNOS	Without CaM	15 ± 2	82 ± 4
WT nNOS	+WT CaM	65 ± 9	32 ± 6
WT nNOS	+E47A CaM	40 ± 6	55 ± 9
K423E nNOS	+ WT CaM	20 ± 5	76 ± 2
Δ2-R1400E_K452N nNOS	+ WT CaM	97 ± 6	5 ± 2
E762R/E816R/E819R nNOS	+ WT CaM	18 ± 8	78 ± 8

Table 2. Fate of the H4B radical following its formation in the Arg hydroxylation reaction.

Table 2. Fate of the H₄B radical following its formation in the Arg hydroxylation reaction.