Published in

American Society for Microbiology, Journal of Bacteriology, 18(195), p. 4112-4120, 2013

DOI: 10.1128/jb.00634-13

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Benzoyl Coenzyme A Pathway-Mediated Metabolism of meta-Hydroxy-Aromatic Acids in Rhodopseudomonas palustris

Journal article published in 2013 by Daniel L. Gall, John Ralph, Timothy J. Donohue ORCID, Daniel R. Noguera
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

ABSTRACT Photoheterotrophic metabolism of two meta -hydroxy-aromatic acids, meta -, para -dihydroxybenzoate (protocatechuate) and meta -hydroxybenzoate, was investigated in Rhodopseudomonas palustris . When protocatechuate was the sole organic carbon source, photoheterotrophic growth in R. palustris was slow relative to cells using compounds known to be metabolized by the benzoyl coenzyme A (benzoyl-CoA) pathway. R. palustris was unable to grow when meta -hydroxybenzoate was provided as a sole source of organic carbon under photoheterotrophic growth conditions. However, in cultures supplemented with known benzoyl-CoA pathway inducers ( para -hydroxybenzoate, benzoate, or cyclohexanoate), protocatechuate and meta -hydroxybenzoate were taken up from the culture medium. Further, protocatechuate and meta -hydroxybenzoate were each removed from cultures containing both meta -hydroxy-aromatic acids at equimolar concentrations in the absence of other organic compounds. Analysis of changes in culture optical density and in the concentration of soluble organic compounds indicated that the loss of these meta -hydroxy-aromatic acids was accompanied by biomass production. Additional experiments with defined mutants demonstrated that enzymes known to participate in the dehydroxylation of para -hydroxybenzoyl-CoA (HbaBCD) and reductive dearomatization of benzoyl-CoA (BadDEFG) were required for metabolism of protocatechuate and meta -hydroxybenzoate. These findings indicate that, under photoheterotrophic growth conditions, R. palustris can degrade meta -hydroxy-aromatic acids via the benzoyl-CoA pathway, apparently due to the promiscuity of the enzymes involved.