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. Author manuscript; available in PMC: 2020 May 15.
Published in final edited form as: J Am Chem Soc. 2019 May 6;141(19):7765–7775. doi: 10.1021/jacs.9b00196

Table 6.

Kinetic Parameters for Nitrite Reductase Activity at pH 5.8 Compared to Previously Published Results and Other Model Complexes or the Native Enzymea

construct rate (s−1) Vmax (M s−1) KM (M) kcat (s−1) kcat/KM (s−1 M−1)
TRIW-H25 4.6 × 10−4 N/A N/A N/A N/A
TRIW-H L19A34 3.5 × 10−2 2.3 ± 0.3 × 10−6 0.24 ± 0.05 0.23 ± 0.03 1.0 ± 0.3
TRIW-δmH 0.12 1.5 ± 0.1 × 105 0.18 ± 0.02 1.5 ± 0.1 8.2 ± 0.1
TRIW-δmH L19A 0.30 1.5 ± 0.1x 105 0.13 ± 0.01 1.5 ± 0.1 11.3 ± 0.1
TRIW-εmH 1.2 × 10−3 N/A N/A N/A N/A
[CuMe2bpa(H2O)(ClO4)]+ on electrode pH 5.545 N/A N/A 1.1 × 103 0.063 57.3
[CuMe2bpa(H2O)(ClO4)]+ in solution pH 5.545 N/A N/A 2.5 × 103 5.3 × 105 0.02
AfCuNiR pH 6.546 N/A N/A 1.5 × 104 620 4.1 × 106
AxCuNiR pH 7.0, 4 °C47 N/A N/A 2.7 × 103 89 3.3 × 105
a

The rate value above refers to the pseudo-first order rate constant for metallopeptide-catalyzed reduction of nitrite by ascorbate in solutions containing 30 mM nitrite and 1.2 mM ascorbate.25