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dc.contributor.authorCreevey, Nicole
dc.contributor.authorMcEwan, A.
dc.contributor.authorHanson, G.
dc.contributor.authorBernhardt, P.
dc.date.accessioned2017-05-03T15:39:32Z
dc.date.available2017-05-03T15:39:32Z
dc.date.issued2008
dc.date.modified2011-10-17T07:25:05Z
dc.identifier.issn00062960
dc.identifier.doi10.1021/bi702444r
dc.identifier.urihttp://hdl.handle.net/10072/38468
dc.description.abstractDimethylsulfide (DMS) dehydrogenase is a complex heterotrimeric enzyme that catalyzes the oxidation of DMS to DMSO and allows Rhodovulum sulfidophilum to grow under photolithotrophic conditions with DMS as the electron donor. The enzyme is a 164 kDa heterotrimer composed of an a-subunit that binds a bis(molybdopterin guanine dinucleotide)Mo cofactor, a polyferredoxin ߭subunit, and a ?-subunit that contains a b-type heme. In this study, we describe the thermodynamic characterization of the redox centers within DMS dehydrogenase using EPR- and UV-visible-monitored potentiometry. Our results are compared with those of other bacterial Mo enzymes such as NarGHI nitrate reductase, selenate reductase, and ethylbenzene dehydrogenase. A remarkable similarity in the redox potentials of all Fe-S clusters is apparent.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoen_AU
dc.publisherACS Publications
dc.publisher.placeUSA
dc.relation.ispartofstudentpublicationY
dc.relation.ispartofpagefrom3770
dc.relation.ispartofpageto3776
dc.relation.ispartofissue12
dc.relation.ispartofjournalBiochemistry
dc.relation.ispartofvolume47
dc.rights.retentionY
dc.subject.fieldofresearchChemical Sciences not elsewhere classified
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchMedical Biochemistry and Metabolomics
dc.subject.fieldofresearchcode039999
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0601
dc.subject.fieldofresearchcode1101
dc.titleThermodynamic Characterization of the Redox Centers within Dimethylsulfide Dehydrogenase
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyrightSelf-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the author[s] for more information.
gro.date.issued2008
gro.hasfulltextNo Full Text
gro.griffith.authorKnight, Nicole


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