Potential early intermediates in anaerobic benzoate degradation by Rhodopseudomonas palustris

@article{Gibson1992PotentialEI,
  title={Potential early intermediates in anaerobic benzoate degradation by Rhodopseudomonas palustris},
  author={Katharine J. Gibson and Janet L. Gibson},
  journal={Applied and Environmental Microbiology},
  year={1992},
  volume={58},
  pages={696 - 698}
}
  • K. Gibson, J. Gibson
  • Published 1 February 1992
  • Chemistry, Medicine
  • Applied and Environmental Microbiology
Alkali-treated extracts of Rhodopseudomonas palustris growing photosynthetically on benzoate were examined by gas chromatography/mass spectrometry for partially reduced benzoate derivatives. Two cyclic dienes, cyclohexa-2,5-diene-1-carboxylate and cyclohexa-1,4-diene-1-carboxylate, were detected. Either compound supported cell growth as effectively as benzoate. These results suggest that these cyclohexadienecarboxylates, probably as their coenzyme A esters, are the initial reduction products… 
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TLDR
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Degradation of aromatic compounds by nonsulfur purple bacteria
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4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation
TLDR
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Small-Molecule Acetylation Controls the Degradation of Benzoate and Photosynthesis in Rhodopseudomonas palustris
This work shows that the BadL protein of Rhodopseudomonas palustris has N-acetyltransferase activity and that this activity is required for the catabolism of benzoate under photosynthetic conditions
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SUMMARY: Rhodopseudomonas palustris was grown on benzoate, cyclohexanecarboxylate or succinate under anaerobic or aerobic conditions. Studies of oxygen uptake by intact bacteria indicated that
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TLDR
The photometabolism of benzoate is accomplished by a novel reductive pathway involving its reduction to cyclohex- 1-ene-1-carboxylate, followed by hydration to 2-hydroxycyclohexanecarboxylates, and after dehydrogenation to2-oxocyclohexAnecar boxylate further hydration results in ring-fission and the production of pimelate.
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TLDR
The very effective uptake of external benzoate can be explained by its conversion to benzoyl CoA immediately after its passage across the cell membrane by simple or facilitated diffusion, which would serve to maintain a downhill concentration gradient between the cell cytoplasm and the cell surroundings, even at very low external Benzoate concentrations.
Purification and properties of benzoate-coenzyme A ligase, a Rhodopseudomonas palustris enzyme involved in the anaerobic degradation of benzoate
TLDR
The kinetic properties of the enzyme match the kinetics of substrate uptake by whole cells and confirm a role for benzoate-CoA ligase in maintaining entry of Benzoate into cells as well as in catalyzing the first step in the anaerobic degradation of benzoates by R. palustris.
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TLDR
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TLDR
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