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Table 3 Catalytic properties of RubisCO enzymes (R. eutropha form I (FI) and R. rubrum form II (FII) associated with nanostructures

From: Synthetic CO2-fixation enzyme cascades immobilized on self-assembled nanostructures that enhance CO2/O2 selectivity of RubisCO

Enzymea Ω b (V c K o/V o K c) k cat b (sec−1) K c b (μM) K o b (μM) K o/K c c
Unbound FI 79 ± 1 2.6 ± 0.5 41 ± 4 1093 ± 141 27
FI-nanotube B 95 ± 3d 1.8 ± 0.1e 53 ± 7 1756 ± 341 33
FI-nanofiber C 88 ± 1d 2.2 ± 0.1e 56 ± 8 1693 ± 383 30
Unbound FII 17 ± 2 1.2 ± 0.1 100 ± 7 96 ± 26 1.0
FII-nanotube B 17 ± 1 0.6 ± 0.2e 120 ± 24 170 ± 41 1.4
FII in nanofiber C 17 ± 1 0.6 ± 0.1e 96 ± 16 95 ± 32 1.0
  1. aAssociation with either of the nanotubes (i.e., A or B) imparted similar properties to both form I (FI) and form II (FII) enzymes
  2. bValues are the mean ± standard deviation (n−1) of at least three independent nanostructure-enzyme complex preparations
  3. cCalculated values
  4. dAn unpaired t test with Ω values obtained from three independent experiments gave p values of 0.0006 and 0.0003 for FI-nanotube B and FI-nanofiber C, respectively, relative to unbound FI
  5. eThese k cat values were calculated based on the initial amounts of enzyme added to constitute nanostructure-RubisCO complexes. They are not significantly different from the value measured with the unbound enzyme, if the percentage recoveries are factored into the calculations (Additional file 1: Table S3c) for each experiment