| Abstrakt: |
It was shown that 2H(+)-K(+)-exchange through H(+)-K(+)-pump composed of H(+)-ATPase complex F0F1 and Trk-system of potassium accumulation, H(+)-K(+)-exchange through H(+)-K(+)-antiport, composed of H(+)-channel F0 and of system with Trk-defect, and H2-production in E. coli grown in anaerobic conditions, change in mutants with defects of F0F1 and potassium transport. In unc-mutant of E. coli AN 936 with defects of c-subunit F0 (M(r) 8,4 kDa) H(+)-K(+)-exchange and H2-production disappeared. Mutants of E. coli TK 509 (2240) with defect of Trk-system not able to perform 2H(+)-K(+)-exchange, performed, however H(+)-K(+)-exchange and H2-production which can be blocked of N, N'-dicyclohexylcarbodiimide (DCCD). In mutant of E. coli Tk 509 (2242) with defects of KdpA-protein of Kdp-system of potassium accumulation, Trk A and Trk D proteins of corresponding systems of potassium accumulation, the H(+)-K(+)-exchange disappeared, while H(+)-formation and H2-production, blocked by DCCD, external osmotic pressure and absence of potassium in the medium, persisted. It is assumed that 2H(+)-K(+)-exchange, H(+)-K(+)-exchange and H2-production are connected, and the membrane-bound format-hydrogenlyase oxidizing format to H2 and CO2, directly take part in interaction with F0F1 and Trk, as well as F0 and defective Trk-system in formation of supercomplexs. It is assumed that the format-hydrogen-lyase can interact with F0F1 without the Trk-system. |
