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Review
. 2003 Nov;69(11):6345-53.
doi: 10.1128/AEM.69.11.6345-6353.2003.

Energy conservation in acetogenic bacteria

Volker Müller  1
Affiliations
Review

Energy conservation in acetogenic bacteria

Volker Müller. Appl Environ Microbiol. 2003 Nov.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Wood-Ljungdahl pathway. Reductants are shown as hydrogen, but electrons can also be derived from oxidation of organic substrates.
FIG. 2.
FIG. 2.
Hypothetical model of energy conservation in acetogens. (A) H+ organisms; (B) Na+ organisms. For explanations, see the text.
FIG. 3.
FIG. 3.
The Na+ F1F0 ATPase of A. woodii. (A) Genomic organization of the atp genes; (B) hypothetical model of the enzyme. Please note that the stoichiometry of subunits c1 and c2/3 is unknown. Residues involved in Na+ binding are indicated.
FIG. 4.
FIG. 4.
Na+-binding site in the Na+ F1F0 ATPase of A. woodii.(A) Na+-binding site in subunits c1 and hairpin one of subunit c2/3. Please note that hairpin two of subunit c1 does not contain the conserved glutamate and, therefore, is not capable of binding Na+. (B) Closer look on the Na+-binding site.
FIG. 5.
FIG. 5.
Rotors of different ATPases. E. coli F1F0 is assumed to have 12 copies of the 8-kDa proteolipid, V1V0 ATPase to have six copies of a duplicated 16-kDa proteolipid in which the H+-translocating glutamate is only conserved in hairpin two. The rotor of A. woodii comprises a mixture of “bacterial-like” 8- and “eukaryal-like” 16-kDa proteolipids with unknown stoichiometry.
FIG. 6.
FIG. 6.
Reduction of the carbon-carbon double bond of phenylacrylate ethers such as caffeate by A. woodii.
See this image and copyright information in PMC

References

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    1. Das, A., and L. G. Ljungdahl. 1997. Composition and primary structure of the F1F0 ATP synthase from the obligately anaerobic bacterium Clostridium thermoaceticum. J. Bacteriol. 179:3746-3755. - PMC - PubMed

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