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. Author manuscript; available in PMC: 2022 May 31.
Published in final edited form as: Dalton Trans. 2021 Aug 4;50(30):10405–10422. doi: 10.1039/d1dt01359a

Table 1.

HydG rates for free CO formation as monitored via single wavelength kinetics experiments (λ = 425 nm, see Fig. 2)

Enzyme Burst phasee (min−1) Biphasic, rate 1 f (min−1) Biphasic, rate 2 f (min−1)

HydGΔEF a 0.0836 ± 0.0022 0.0658 ± 0.0034 0.0370 ± 0.0079
HydGEF b 0.0973 ± 0.0193 0.0637 ± 0.0046 0.0348 ± 0.0052
Dangler loaded HydGΔEF c 0.0941 ± 0.0036 0.0640 ± 0.0001 0.0529 ± 0.0032
H272A HydGΔEF d 0.0036 ± 0.0001 N/A N/A
a

WT traditionally reconstituted HydGΔEF with 7.54 ± 0.48 Fe per protein.

b

WT traditionally reconstituted HydGEF with 7.38 ± 0.40 Fe per protein.

c

WT dangler reconstituted HydGΔEF with 8.23 ± 0.43 Fe per protein.

d

Traditionally reconstituted H272A HydGΔEF with 7.2 ± 0.4 Fe per protein. N/A = not applicable.

e

Burst phase rate determined by linear fit to data between 0–5 min.

f

These rates come from biphasic exponential fits to the same data, using all data points from 0 to 120 min.