This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Becher, B Articles by Müller, V Search for Related Content PubMed PubMed Citation Articles by Becher, B Articles by Müller, V

 Previous Article  |  Next Article 

J Bacteriol. 1994 May; 176(9): 2543-2550

Delta mu Na+ drives the synthesis of ATP via an delta mu Na(+)-translocating F1F0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei Gö1.

Institut für Mikrobiologie, Georg-August-Universität, Göttingen, Germany.

ABSTRACT

Methanosarcina mazei Gö1 couples the methyl transfer from methyl-tetrahydromethanopterin to 2-mercaptoethanesulfonate (coenzyme M) with the generation of an electrochemical sodium ion gradient (delta mu Na+) and the reduction of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreoninephosphate with the generation of an electrochemical proton gradient (delta muH+). Experiments with washed inverted vesicles were performed to investigate whether both ion gradients are used directly for the synthesis of ATP. delta mu Na+ and delta mu H+ were both able to drive the synthesis of ATP in the vesicular system. ATP synthesis driven by heterodisulfide reduction (delta mu H+) or an artificial delta pH was inhibited by the protonophore SF6847 but not by the sodium ionophore ETH157, whereas ETH157 but not SF6847 inhibited ATP synthesis driven by a chemical sodium ion gradient (delta pNa) as well as the methyl transfer reaction (delta mu Na+). Inhibition of the Na+/H+ antiporter led to a stimulation of ATP synthesis driven by the methyl transfer reaction (delta mu Na+), as well as by delta pNa. These experiments indicate that delta mu Na+ and delta mu H+ drive the synthesis of ATP via an Na(+)- and an H(+)-translocating ATP synthase, respectively. Inhibitor studies were performed to elucidate the nature of the ATP synthase(s) involved. delta pH-driven ATP synthesis was specifically inhibited by bafilomycin A1, whereas delta pNa-driven ATP synthesis was exclusively inhibited by 7-chloro-4-nitro-2-oxa-1,3-diazole, azide, and venturicidin. These results are evidence for the presence of an F(1)F(0)-ATP synthase in addition to the A(1)A(0)-ATP synthase in membranes of M. Mazei Gö1 and suggest that the F(1)F(0)-type enzyme is an Na+-translocating ATP synthase, whereas the A(1)A(0)-ATP synthase uses H+ as the coupling ion.

This article has been cited by other articles:

• Ruppert, C., Kavermann, H., Wimmers, S., Schmid, R., Kellermann, J., Lottspeich, F., Huber, H., Stetter, K. O., Muller, V. (1999). The Proteolipid of the A1A0 ATP Synthase from Methanococcus jannaschii Has Six Predicted Transmembrane Helices but Only Two Proton-translocating Carboxyl Groups. J. Biol. Chem. 274: 25281-25284 [Abstract] [Full Text]  
• Schafer, G., Engelhard, M., Muller, V. (1999). Bioenergetics of the Archaea. Microbiol. Mol. Biol. Rev. 63: 570-620 [Abstract] [Full Text]  
• Ide, T., Bäumer, S., Deppenmeier, U. (1999). Energy Conservation by the H2:Heterodisulfide Oxidoreductase from Methanosarcina mazei Go1: Identification of Two Proton-Translocating Segments. J. Bacteriol. 181: 4076-4080 [Abstract] [Full Text]  
• Kakinuma, Y. (1998). Inorganic Cation Transport and Energy Transduction in Enterococcus hirae and Other Streptococci. Microbiol. Mol. Biol. Rev. 62: 1021-1045 [Abstract] [Full Text]  
• Ruppert, C., Wimmers, S., Lemker, T., Müller, V. (1998). The A1Ao ATPase from Methanosarcina mazei: Cloning of the 5' End of the aha Operon Encoding the Membrane Domain and Expression of the Proteolipid in a Membrane-Bound Form in Escherichia coli. J. Bacteriol. 180: 3448-3452 [Abstract] [Full Text]  
• Wilms, R., Freiberg, C., Wegerle, E., Meier, I., Mayer, F., Muller, V. (1996). Subunit Structure and Organization of the Genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Go1. J. Biol. Chem. 271: 18843-18852 [Abstract] [Full Text]