By Terry Krulwich (Eds.)
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Additional resources for Bacterial Energetics. A Treatise on Structure and Function
Chem. 258, 9159-9165. Miller, M. , and Gennis, R. B. (1985). The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli. J. Biol. Chem. 260, 14003-14008. Mitchell, P. (1966). Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Rev. 41, 445-502. Mitchell, P. (1976). Possible molecular mechanism of the proton motive function of cytochrome systems. J. Theor. Biol. 62, 327-367. Mitchell, P. (1987). A new redox loop formality involving metal-catalysed hydroxide-ion translocation.
Hilpert et al. (1984) have shown that the membranes of P. modestum contained a large amount of ATPase which was specifically activated by Na-1". Inverted membrane vesicles derived from this organism accumulated Na+ in response to ATP hydrolysis, which was inhibited by monensin but not by FCCP. These results indicate that the translocation of Na + was directly coupled to ATP hydrolysis by Na + -ATPase. Furthermore, the two Na + pumps present in the membrane vesicles were shown to be energetically coupled, that is, monensin-sensitive ATP synthesis by malonylCoA decarboxylation and monensin-sensitive acetyl-CoA carboxylation by ATP hydrolysis.
By the addition of NADH in the presence of Q-l, the Δψ was generated concomitantly with the formation of QH 2 , which was completely dependent on Na4" and was inhibited by HQNO. When menadione, which accepts electrons from the FAD-containing β subunit, was used as the electron acceptor, no significant Δψ was generated. Thus, the Na+-dependent and HQNO-sensitive reaction catalyzed by the FMN-containing a subunit directly participated in the generation of Δψ, indicating that this reaction step is directly coupled to the translocation of Na4" (Fig.
Bacterial Energetics. A Treatise on Structure and Function by Terry Krulwich (Eds.)