Syntrophic butyrate and propionate oxidation processes : from genomes to reaction mechanisms

Müller, Nicolai; Worm, Petra; Schink, Bernhard; Stams, Alfons J. M.; Plugge, Caroline M.

Syntrophic butyrate and propionate oxidation processes : from genomes to reaction mechanisms

Dateien

2010_Mueller_489_499.pdfGröße: 336.18 KBDownloads: 2385

Datum

2010

Autor:innen

Müller, Nicolai

Worm, Petra

Schink, Bernhard

Stams, Alfons J. M.

Plugge, Caroline M.

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Environmental Microbiology Reports. 2010, 2(4), pp. 489-499. eISSN 1758-2229. Available under: doi: 10.1111/j.1758-2229.2010.00147.x

Zusammenfassung

In anoxic environments such as swamps, rice fields and sludge digestors, syntrophic microbial communities are important for decomposition of organic matter to CO2 and CH4. The most difficult step is the fermentative degradation of short-chain fatty acids such as propionate and butyrate. Conversion of these metabolites to acetate, CO2, formate and hydrogen is endergonic under standard conditions and occurs only if methanogens keep the concentrations of these intermediate products low. Butyrate and propionate degradation pathways include oxidation steps of comparably high redox potential, i.e. oxidation of butyryl-CoA to crotonyl-CoA and of succinate to fumarate, respectively, that require investment of energy to release the electrons as hydrogen or formate. Although investigated for several decades, the biochemistry of these reactions is still not completely understood. Genome analysis of the butyrateoxidizing Syntrophomonas wolfei and Syntrophus aciditrophicus and of the propionate-oxidizing Syntrophobacter fumaroxidans and Pelotomaculum thermopropionicum reveals the presence of energytransforming protein complexes. Recent studies indicated that S. wolfei uses electron-transferring flavoproteins coupled to a menaquinone loop to drive butyryl-CoA oxidation, and that S. fumaroxidans uses a periplasmic formate dehydrogenase, cytochrome b:quinone oxidoreductases, a menaquinone loop and a cytoplasmic fumarate reductase to drive energydependent succinate oxidation. Furthermore, we propose that homologues of the Thermotoga maritima bifurcating [FeFe]-hydrogenase are involved in NADH oxidation by S. wolfei and S. fumaroxidans to form hydrogen.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

MÜLLER, Nicolai, Petra WORM, Bernhard SCHINK, Alfons J. M. STAMS, Caroline M. PLUGGE, 2010. Syntrophic butyrate and propionate oxidation processes : from genomes to reaction mechanisms. In: Environmental Microbiology Reports. 2010, 2(4), pp. 489-499. eISSN 1758-2229. Available under: doi: 10.1111/j.1758-2229.2010.00147.x

BibTex

@article{Muller2010Syntr-7488,
  year={2010},
  doi={10.1111/j.1758-2229.2010.00147.x},
  title={Syntrophic butyrate and propionate oxidation processes : from genomes to reaction mechanisms},
  number={4},
  volume={2},
  journal={Environmental Microbiology Reports},
  pages={489--499},
  author={Müller, Nicolai and Worm, Petra and Schink, Bernhard and Stams, Alfons J. M. and Plugge, Caroline M.}
}

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Universitätsbibliographie

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