Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens

Detalhes bibliográficos
Autor(a) principal: Sedano-Núñez, Vicente T.
Data de Publicação: 2018
Outros Autores: Boeren, Sjef, Stams, Alfons Johannes Maria, Plugge, Caroline M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/55077
Resumo: Syntrophobacter fumaroxidans is a sulfatereducing bacterium able to grow on propionate axenically or in syntrophic interaction with methanogens or other sulfatereducing 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. This article is protected by copyright
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spelling Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogensSyntrophysulfate-reducing bacteriapropionate oxidationinterspecies electron transferreverse electron transporthydrogenasesformate dehydrogenasesScience & TechnologySyntrophobacter fumaroxidans is a sulfatereducing bacterium able to grow on propionate axenically or in syntrophic interaction with methanogens or other sulfatereducing 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. This article is protected by copyrightThis research was supported by the Dutch Technology Foundation (STW) (project 11603), which is part of the Netherlands Organization for Scientific Research (NWO), and which is partly funded by the Ministry of Economic Affairs. Research of AJMS is supported by the European Research Council (ERC grant 323009) and the Gravitation grant (024.002.002) of the Netherlands Ministry of Education, Cultureand Science.info:eu-repo/semantics/publishedVersionWiley-BlackwellUniversidade do MinhoSedano-Núñez, Vicente T.Boeren, SjefStams, Alfons Johannes MariaPlugge, Caroline M.2018-052018-05-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/55077engSedano-Núñez, Vicente T.; Boeren, Sjef; Stams, A. J. M.; Plugge, Caroline M., Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens. Environmental Microbiology, 20(5), 1842-1856, 20181462-29121462-292010.1111/1462-2920.1411929611893http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:34:19Zoai:repositorium.sdum.uminho.pt:1822/55077Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:29:59.510881Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv 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
spellingShingle Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens
Sedano-Núñez, Vicente T.
Syntrophy
sulfate-reducing bacteria
propionate oxidation
interspecies electron transfer
reverse electron transport
hydrogenases
formate dehydrogenases
Science & Technology
title_short 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_sort Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens
author Sedano-Núñez, Vicente T.
author_facet Sedano-Núñez, Vicente T.
Boeren, Sjef
Stams, Alfons Johannes Maria
Plugge, Caroline M.
author_role author
author2 Boeren, Sjef
Stams, Alfons Johannes Maria
Plugge, Caroline M.
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Sedano-Núñez, Vicente T.
Boeren, Sjef
Stams, Alfons Johannes Maria
Plugge, Caroline M.
dc.subject.por.fl_str_mv Syntrophy
sulfate-reducing bacteria
propionate oxidation
interspecies electron transfer
reverse electron transport
hydrogenases
formate dehydrogenases
Science & Technology
topic Syntrophy
sulfate-reducing bacteria
propionate oxidation
interspecies electron transfer
reverse electron transport
hydrogenases
formate dehydrogenases
Science & Technology
description Syntrophobacter fumaroxidans is a sulfatereducing bacterium able to grow on propionate axenically or in syntrophic interaction with methanogens or other sulfatereducing 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. This article is protected by copyright
publishDate 2018
dc.date.none.fl_str_mv 2018-05
2018-05-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/55077
url http://hdl.handle.net/1822/55077
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Sedano-Núñez, Vicente T.; Boeren, Sjef; Stams, A. J. M.; Plugge, Caroline M., Comparative proteome analysis of propionate degradation by Syntrophobacter fumaroxidans in pure culture and in coculture with methanogens. Environmental Microbiology, 20(5), 1842-1856, 2018
1462-2912
1462-2920
10.1111/1462-2920.14119
29611893
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley-Blackwell
publisher.none.fl_str_mv Wiley-Blackwell
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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