Formic acid synthesis using CO₂ as raw material: Techno-economic and environmental evaluation and market potential

The future of carbon dioxide utilisation (CDU) processes, depend on (i) the future demand of synthesised products with CO₂, (ii) the availability of captured and anthropogenic CO₂, (iii) the overall CO₂ not emitted because of the use of the CDU process, and (iv) the economics of the plant. The current work analyses the mentioned statements through different technological, economic and environmental key performance indicators to produce formic acid from CO₂, along with their potential use and penetration in the European context. Formic acid is a well-known chemical that has potential as hydrogen carrier and as fuel for fuel cells. This work utilises process flow modelling, with simulations developed in CHEMCAD, to obtain the energy and mass balances, and the purchase equipment cost of the formic acid plant. Through a financial analysis, with the net present value as selected metric, the price of the tonne of formic acid and of CO₂ are varied to make the CDU project financially feasible. According to our research, the process saves CO₂ emissions when compared to its corresponding conventional process, under specific conditions. The success or effectiveness of the CDU process will also depend on other technologies and/or developments, like the availability of renewable electricity and steam

The Kdp-ATPase of Escherichia coli

The kdpFABC operon of Escherichia coli consists of the four structural genes kdpF, kdpA, kdpB, and kdpC. Expression of the kdpF gene was demonstrated using minicells of E. coli. In addition, it was shown that the KdpF subunit remains associated with the purified complex. Although KdpF is not essential in vivo, the purified complex lacking KdpF exhibits hardly any K+-stimulated ATPase activity. This clearly demonstrates that the KdpF subunit is stabilizing the transport complex. Charge translocation by the purified Kdp-ATPase was measured with the potential-sensitive dye DiSC3(5) using proteoliposomes. Upon addition of ATP a fluorescence quench was observed indicating the buildup of a negative potential inside the proteoliposomes. Using the Kdp-ATPase derived from a mutant strain, in which the Km value for K+ (1,2 mM) was almost identical to that of Rb+ (1.4 mM), the same fluorescence quench was observed when K+ or Rb+ were present in the lumen of the proteoliposomes. These data clearly indicate that the Kdp-ATPase transports K+ in an electrogenic manner. In order to identify the binding site(s) for the inhibitor concanamycin A within the Kdp complex, concanamycin A was synthesized. Using this compound labeling of KdpA and KdpB, but not of KdpC, could be shown with the purified complex. When everted vesicles were used only KdpB could be labeled