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http://purl.uniprot.org/citations/25512312http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25512312http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25512312http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25512312http://www.w3.org/2000/01/rdf-schema#comment"Desulfitobacterium dehalogenans is able to grow by organohalide respiration using 3-chloro-4-hydroxyphenyl acetate (Cl-OHPA) as an electron acceptor. We used a combination of genome sequencing, biochemical analysis of redox active components, and shotgun proteomics to study elements of the organohalide respiratory electron transport chain. The genome of Desulfitobacterium dehalogenans JW/IU-DC1(T) consists of a single circular chromosome of 4,321,753 bp with a GC content of 44.97%. The genome contains 4,252 genes, including six rRNA operons and six predicted reductive dehalogenases. One of the reductive dehalogenases, CprA, is encoded by a well-characterized cprTKZEBACD gene cluster. Redox active components were identified in concentrated suspensions of cells grown on formate and Cl-OHPA or formate and fumarate, using electron paramagnetic resonance (EPR), visible spectroscopy, and high-performance liquid chromatography (HPLC) analysis of membrane extracts. In cell suspensions, these components were reduced upon addition of formate and oxidized after addition of Cl-OHPA, indicating involvement in organohalide respiration. Genome analysis revealed genes that likely encode the identified components of the electron transport chain from formate to fumarate or Cl-OHPA. Data presented here suggest that the first part of the electron transport chain from formate to fumarate or Cl-OHPA is shared. Electrons are channeled from an outward-facing formate dehydrogenase via menaquinones to a fumarate reductase located at the cytoplasmic face of the membrane. When Cl-OHPA is the terminal electron acceptor, electrons are transferred from menaquinones to outward-facing CprA, via an as-yet-unidentified membrane complex, and potentially an extracellular flavoprotein acting as an electron shuttle between the quinol dehydrogenase membrane complex and CprA."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.org/dc/terms/identifier"doi:10.1128/JB.02370-14"xsd:string
http://purl.uniprot.org/citations/25512312http://purl.org/dc/terms/identifier"doi:10.1128/jb.02370-14"xsd:string
http://purl.uniprot.org/citations/25512312http://purl.org/dc/terms/identifier"doi:10.1128/jb.02370-14"xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Chain P."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Chain P."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Chain P."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Goodwin L."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Goodwin L."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Goodwin L."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Boeren S."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Boeren S."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Boeren S."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Hagen W.R."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Hagen W.R."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"Hagen W.R."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"de Vos W.M."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"de Vos W.M."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"de Vos W.M."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"van der Oost J."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"van der Oost J."xsd:string
http://purl.uniprot.org/citations/25512312http://purl.uniprot.org/core/author"van der Oost J."xsd:string