Skip to main content


Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Fig. 6 | Biotechnology for Biofuels

Fig. 6

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

Fig. 6

Reaction velocity measurements of R. eutropha form I RubisCO as a function of CO2 concentration in the presence (open circles) or absence (closed circles) of saturating levels of oxygen (i.e., 1230 μM). a Michaelis–Menten curves for carboxylation activities measured with unbound R. eutropha form I RubisCO. b Michaelis–Menten curves for carboxylation activities measured with nanotube B-form I RubisCO complexes. The extent of oxygen inhibition for each enzyme preparation is indicated (double-headed arrows). The K O (K I) for O2 was enhanced about 1.6-fold for the nanotube B-form I enzyme complex compared to the unbound enzyme (see Table 3 for kinetic constants). The average value and error bar for each data point was calculated with values obtained from two independent assays (with different preparations) performed with identical CO2 concentrations

Back to article page