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Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens
Syntrophobacter fumaroxidans is a sulfate‐reducing bacterium able to grow on propionate axenically or in syntrophic interaction with methanogens or other sulfate‐reducing bacteria. We performed a proteome analysis of S. fumaroxidans growing with propionate axenically with sulfate or fumarate, and in...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5947623/ https://www.ncbi.nlm.nih.gov/pubmed/29611893 http://dx.doi.org/10.1111/1462-2920.14119 |
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author | Sedano‐Núñez, Vicente T. Boeren, Sjef Stams, Alfons J. M. Plugge, Caroline M. |
author_facet | Sedano‐Núñez, Vicente T. Boeren, Sjef Stams, Alfons J. M. Plugge, Caroline M. |
author_sort | Sedano‐Núñez, Vicente T. |
collection | PubMed |
description | Syntrophobacter fumaroxidans is a sulfate‐reducing bacterium able to grow on propionate axenically or in syntrophic interaction with methanogens or other sulfate‐reducing bacteria. We performed a proteome analysis of S. fumaroxidans growing with propionate axenically with sulfate or fumarate, and in syntrophy with Methanospirillum hungatei, Methanobacterium formicicum or Desulfovibrio desulfuricans. Special attention was put on the role of hydrogen and formate in interspecies electron transfer (IET) and energy conservation. Formate dehydrogenase Fdh1 and hydrogenase Hox were the main confurcating enzymes used for energy conservation. In the periplasm, Fdh2 and hydrogenase Hyn play an important role in reverse electron transport associated with succinate oxidation. Periplasmic Fdh3 and Fdh5 were involved in IET. The sulfate reduction pathway was poorly regulated and many enzymes associated with sulfate reduction (Sat, HppA, AprAB, DsrAB and DsrC) were abundant even at conditions where sulfate was not present. Proteins similar to heterodisulfide reductases (Hdr) were abundant. Hdr/Flox was detected in all conditions while HdrABC/HdrL was exclusively detected when sulfate was available; these complexes most likely confurcate electrons. Our results suggest that S. fumaroxidans mainly used formate for electron release and that different confurcating mechanisms were used in its sulfidogenic metabolism. |
format | Online Article Text |
id | pubmed-5947623 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-59476232018-05-17 Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens Sedano‐Núñez, Vicente T. Boeren, Sjef Stams, Alfons J. M. Plugge, Caroline M. Environ Microbiol Research Articles Syntrophobacter fumaroxidans is a sulfate‐reducing bacterium able to grow on propionate axenically or in syntrophic interaction with methanogens or other sulfate‐reducing bacteria. We performed a proteome analysis of S. fumaroxidans growing with propionate axenically with sulfate or fumarate, and in syntrophy with Methanospirillum hungatei, Methanobacterium formicicum or Desulfovibrio desulfuricans. Special attention was put on the role of hydrogen and formate in interspecies electron transfer (IET) and energy conservation. Formate dehydrogenase Fdh1 and hydrogenase Hox were the main confurcating enzymes used for energy conservation. In the periplasm, Fdh2 and hydrogenase Hyn play an important role in reverse electron transport associated with succinate oxidation. Periplasmic Fdh3 and Fdh5 were involved in IET. The sulfate reduction pathway was poorly regulated and many enzymes associated with sulfate reduction (Sat, HppA, AprAB, DsrAB and DsrC) were abundant even at conditions where sulfate was not present. Proteins similar to heterodisulfide reductases (Hdr) were abundant. Hdr/Flox was detected in all conditions while HdrABC/HdrL was exclusively detected when sulfate was available; these complexes most likely confurcate electrons. Our results suggest that S. fumaroxidans mainly used formate for electron release and that different confurcating mechanisms were used in its sulfidogenic metabolism. John Wiley and Sons Inc. 2018-04-23 2018-05 /pmc/articles/PMC5947623/ /pubmed/29611893 http://dx.doi.org/10.1111/1462-2920.14119 Text en © 2018 The Authors. Environmental Microbiology published by Society for Applied Microbiology and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Research Articles Sedano‐Núñez, Vicente T. Boeren, Sjef Stams, Alfons J. M. Plugge, Caroline M. Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens |
title | Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens |
title_full | Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens |
title_fullStr | Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens |
title_full_unstemmed | Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens |
title_short | Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens |
title_sort | comparative proteome analysis of propionate degradation by syntrophobacter fumaroxidans in pure culture and in coculture with methanogens |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5947623/ https://www.ncbi.nlm.nih.gov/pubmed/29611893 http://dx.doi.org/10.1111/1462-2920.14119 |
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