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. Author manuscript; available in PMC: 2012 May 24.
Published in final edited form as: Biochemistry. 2011 May 3;50(20):4281–4290. doi: 10.1021/bi200341b

Table 5.

Comparison of kinetic parameters for various sGC β1 mutants in α1β1 and H-NOX domains at 37 °C

Protein Mutation obs Kon O2 (μM−1 s−1) Kox (s−1)
α1β1 wt N.O.a N.O.
β1 P118A N.O. N.O.
β1 I145Y N.O. N.O.
β1(1–385) wt N.O. 0.00029 ± 0.00002
β1 P118A N.O. 17.6 ± 0.3b
β1 I145Y ~0.00004c 0.00020c
β1 P118AI145Y 0.00012 ± 0.00003 0.00062 ± 0.00025
β1(1–194) wt N.O. 0.00121d
β1 P118A N.O. 0.1950 ± 0.006
β1 I145Y N.O. 0.0022 ± 0.0005
a

N.O., not observed;

b

Rate measured and reported at 10 °C;

c

Rates from (32);

d

Rates from (6).