Both authors contributed equally.
Syntrophic butyrate and propionate oxidation processes: from genomes to reaction mechanisms
Article first published online: 3 MAR 2010
© 2010 Society for Applied Microbiology and Blackwell Publishing Ltd
Environmental Microbiology Reports
Special Issue: Symbiosis. Editors: Professors Paola Bonfante, Karen Visick, and Moriya Ohkuma
Volume 2, Issue 4, pages 489–499, August 2010
How to Cite
Müller, N., Worm, P., Schink, B., Stams, A. J. M. and Plugge, C. M. (2010), Syntrophic butyrate and propionate oxidation processes: from genomes to reaction mechanisms. Environmental Microbiology Reports, 2: 489–499. doi: 10.1111/j.1758-2229.2010.00147.x
- Issue published online: 16 JUL 2010
- Article first published online: 3 MAR 2010
- Received 3 November, 2009; accepted 9 January, 2010.
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 butyrate-oxidizing Syntrophomonas wolfei and Syntrophus aciditrophicus and of the propionate-oxidizing Syntrophobacter fumaroxidans and Pelotomaculum thermopropionicum reveals the presence of energy-transforming 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 energy-dependent 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.