써모코커스 온누리누스 NA1 균주의 개미산 에너지 대사

Abstract

Previously, we reported that several hyperthermophilic archaeal strains belonging to Thermoccocales including T. onnurineus NA1 were able to grow on formate and produce a substantial amount of H2. fdh2-mfh2-mnh2 gene cluster was reported to be responsible for formate-oxidizing, hydrogen-producing growth, and multisubunit monovalent cation/proton antiporter encoded by mnh2 has been thought to participate in formate-dependent energy conservation for the synthesis of ATPs. The hydrogenase gene cluster was unique in retaining a putative cation/proton antiporter. The tripartite modular organization of group 4 hydrogenase could be found in many archaeal genomes, however, there is no report to unveil the physiological role of multisubunit monovalent cation/proton antiporter participating in mediating the electron relay of the respiratory chain to date. The multisubunit monovalent cation/proton antiporter (Mrp homologues) has been mainly studied in bacteria at a physiological function of alkaline pH homeostasis and Na+ resistance, cell sporulation, symbiotic nitrogen fixation, arsenite resistance and bile salt resistance. Here, we try to address the identity of chemiosmotic ion to couple formate oxidation to ATP synthesis in the anaerobic respiratory mechanism of formate oxidation. Additionally, the physiological role of the multisubunit monovalent cation/proton antiporter related with ATP synthesis was considered. be responsible for formate-oxidizing, hydrogen-producing growth, and multisubunit monovalent cation/proton antiporter encoded by mnh2 has been thought to participate in formate-dependent energy conservation for the synthesis of ATPs. The hydrogenase gene cluster was unique in retaining a putative cation/proton antiporter. The tripartite modular organization of group 4 hydrogenase could be found in many archaeal genomes, however, there is no report to unveil the physiological role of multisubunit monovalent cation/proton antiporter participating in mediating the electron relay of the respiratory chain to date. The multisubunit monovalent cation/proton antiporter (Mrp homologues) has been mainly studied in bacteria at a physiological function of alkaline pH homeostasis and Na+ resistance, cell sporulation, symbiotic nitrogen fixation, arsenite resistance and bile salt resistance. Here, we try to address the identity of chemiosmotic ion to couple formate oxidation to ATP synthesis in the anaerobic respiratory mechanism of formate oxidation. Additionally, the physiological role of the multisubunit monovalent cation/proton antiporter related with ATP synthesis was considered.