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Proteome-based new insights into dimethyl sulfide metabolism of Hyphomicrobium denitrificans

ABSTRACT: To get further insights in the dimethyl sulfide metabolism of Hyphomicrobium denitrificans, a LC-MS proteomic approach was used. The total protein of three biological replicates of H. denitrificans grown on dimethyl sulfide was compared with three biological replicates grown on dimethylamine. This approach resulted in the identification of several new proteins with a potential involvement in dimethyl sulfide degradation.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Hyphomicrobium Denitrificans Atcc 51888

SUBMITTER: Marc Sylvester

LAB HEAD: Christiane Dahl

PROVIDER: PXD009030 | Pride | 2018-06-14

REPOSITORIES: Pride

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			Action	DRS
	170510_P_202_CD_Pool2_Denitri_170627.pdResult	Other
	170510_P_202_CD_Pool2_Denitri_170627.pdResultView	Other
	170510_P_202_CD_Pool2_Denitri_170627.pep.xml	Pepxml
	170510_P_202_CD_Pool2_Denitri_170627.prot.xml	Xml
	170513_P_202_CD_042.raw	Raw

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Publications

A novel bacterial sulfur oxidation pathway provides a new link between the cycles of organic and inorganic sulfur compounds.

Koch Tobias T Dahl Christiane C

The ISME journal 20180621 10

Dimethylsulfide (DMS) plays a globally significant role in carbon and sulfur cycling and impacts Earth's climate because its oxidation products serve as nuclei for cloud formation. While the initial steps of aerobic DMS degradation and the fate of its carbon atoms are reasonably well documented, oxidation of the contained sulfur is largely unexplored. Here, we identified a novel pathway of sulfur compound oxidation in the ubiquitously occurring DMS-degrader Hyphomicrobium denitrificans X<sup>T</ ...[more]

PMID: 29930335

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