. Author manuscript; available in PMC: 2009 Oct 20.

Published in final edited form as: Biochemistry. 2005 Dec 27;44(51):16866–16874. doi: 10.1021/bi051898d

Table 3.

Extrapolated rate of the reductive half-reaction with mutant or wild type MSOX and L-proline at pH > pK_a

	k_max (min⁻¹)	pK_a	pK_b
Tyr317Phe^a	0.69 ± 0.01	8.9 ± 0.1	(~10.5)
wild type^b	13.4 ±1.6	8.0 ± 0.1 (7.9 ± 0.1)	-

Values for k_max and pK_a for the mutant are based on a fit of the data at pH ≤ 9.6 to equation 2, as described in the text. An approximate value for pK_b was obtained by fitting the entire data set to equation 3 with C = k_max and pK_a = 8.9.

Values for wild type enzyme are from previous kinetic studies reported by Zhao and Jorns in the pH range from 6.5 to 9.0 (14). The pK_a value shown in parentheses was obtained by spectral titration (14).