Extended Data Table 1 Catalytic properties of CODHs and FDHs

From: Molar-scale formate production via enzymatic hydration of industrial off-gases

 

Name

Mediator

Specific activitya

KM for mediators

kcat

kcat/KM

(U·mg‒1)

(mM)

(sec‒1)

(mM‒1·sec‒1)

CO oxidation

ChCODH2

BVox

510 ± 23

1.4 ± 0.1

620 ± 7.3

430 ± 15

EVox

290 ± 4.6

3.0 ± 0.02

300 ± 6.4

98 ± 2.1

NAD+

ND

ND

ND

ND

ChCODH2 A559W

BVox

1,400 ± 29

1.6 ± 0.05

1,500 ± 27

910 ± 14

EVox

560 ± 8.5

2.6 ± 0.1

550 ± 5.1

210 ± 8.0

NAD+

ND

ND

ND

ND

ChCODH4

BVox

42 ± 0.36

1.3 ± 0.2

41 ± 1.9

32 ± 2.1

EVox

17 ± 0.32

1.6 ± 0.1

19 ± 0.7

12 ± 0.52

NAD+

ND

ND

ND

ND

ToCODH

BVox

170 ± 1.9

2.2 ± 0.1

190 ± 1.6

84 ± 1.4

EVox

61 ± 0.73

3.5 ± 0.2

63 ± 1.3

18 ± 0.62

NAD+

ND

ND

ND

ND

CO2 reduction

MeFDH1

BVred

1.3 ± 0.2

0.015 ± 0.003

2.0 ± 0.2

130 ± 3.5

EVred

66 ± 1.2

0.053 ± 0.004

120 ± 4.8

2,200 ± 79

NADH

1.2 ± 0.1

0.028 ± 0.003

1.8 ± 0.1

65 ± 3.2

RcFDH

BVred

ND

ND

ND

ND

EVred

4.2 ± 0.1

0.027 ± 0.002

6.2 ± 0.2

230 ± 11

NADH

ND

ND

ND

ND

TsFDH

BVred

ND

ND

ND

ND

EVred

ND

ND

ND

ND

NADH

ND

ND

ND

ND

  1. Kinetic properties of the associated enzymes were quantified under the given enzymatic reaction conditions.
  2. aSpecific activities were determined at 20 mM mediator in sodium phosphate buffer saturated with CO (30 °C, pH 6.5). Values are the means ± standard variation, n = 3.
  3. * Kinetic data were assayed at 30 °C, pH 6.5. The kinetic parameters were calculated by fitting the initial rates obtained at six different BV/EV concentrations (0.0625–32 mM) to the Hanes–Woolf equation using SigmaPlot 10.0. All enzymatic activities were determined in triplicate (see details in the Methods section).
  4. † The values of kcat were calculated from Vmax for BV and EV.
  5. ND was noted when the specific activity was under 1 U·mg‒1.
Back to article page