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dc.contributor.authorWarelow, Thomas P.
dc.contributor.authorOke, Muse
dc.contributor.authorSchoepp-Cothenet, Barbara
dc.contributor.authorDahl, Jan U.
dc.contributor.authorBruselat, Nicole
dc.contributor.authorSivalingam, Ganesh N.
dc.contributor.authorLeimkuehler, Silke
dc.contributor.authorThalassinos, Konstantinos
dc.contributor.authorKappler, Ulrike
dc.contributor.authorNaismith, James H.
dc.contributor.authorSantini, Joanne M.
dc.date.accessioned2014-05-02T10:01:00Z
dc.date.available2014-05-02T10:01:00Z
dc.date.issued2013-08-30
dc.identifier115258036
dc.identifier711a57b2-95b9-4580-9ba4-bc87cc926e90
dc.identifier000323880200016
dc.identifier84883383174
dc.identifier.citationWarelow , T P , Oke , M , Schoepp-Cothenet , B , Dahl , J U , Bruselat , N , Sivalingam , G N , Leimkuehler , S , Thalassinos , K , Kappler , U , Naismith , J H & Santini , J M 2013 , ' The respiratory arsenite oxidase : structure and the role of residues surrounding the rieske cluster ' , PLoS One , vol. 8 , no. 8 , 72535 . https://doi.org/10.1371/journal.pone.0072535en
dc.identifier.issn1932-6203
dc.identifier.urihttps://hdl.handle.net/10023/4693
dc.descriptionStructural work was supported by grants from The Scottish Funding Council [grant number SULSA (to JHN)] and BBSRC [grant number BB/S/B14450 (to JHN).en
dc.description.abstractThe arsenite oxidase (Aio) from the facultative autotrophic Alphaproteobacterium Rhizobium sp. NT-26 is a bioenergetic enzyme involved in the oxidation of arsenite to arsenate. The enzyme from the distantly related heterotroph, Alcaligenes faecalis, which is thought to oxidise arsenite for detoxification, consists of a large alpha subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small beta subunit (AioB) which contains a Rieske 2Fe-2S cluster. The successful heterologous expression of the NT-26 Aio in Escherichia coli has resulted in the solution of its crystal structure. The NT-26 Aio, a heterotetramer, shares high overall similarity to the heterodimeric arsenite oxidase from A. faecalis but there are striking differences in the structure surrounding the Rieske 2Fe-2S cluster which we demonstrate explains the difference in the observed redox potentials (+225 mV vs. +130/160 mV, respectively). A combination of site-directed mutagenesis and electron paramagnetic resonance was used to explore the differences observed in the structure and redox properties of the Rieske cluster. In the NT-26 AioB the substitution of a serine (S126 in NT-26) for a threonine as in the A. faecalis AioB explains a -20 mV decrease in redox potential. The disulphide bridge in the A. faecalis AioB which is conserved in other betaproteobacterial AioB subunits and the Rieske subunit of the cytochrome bc(1) complex is absent in the NT-26 AioB subunit. The introduction of a disulphide bridge had no effect on Aio activity or protein stability but resulted in a decrease in the redox potential of the cluster. These results are in conflict with previous data on the betaproteobacterial AioB subunit and the Rieske of the bc(1) complex where removal of the disulphide bridge had no effect on the redox potential of the former but a decrease in cluster stability was observed in the latter.
dc.format.extent10
dc.format.extent745183
dc.language.isoeng
dc.relation.ispartofPLoS Oneen
dc.subjectIron-sulfur proteinen
dc.subjectEscherichia-colien
dc.subjectBc(1) complexen
dc.subjectAlcaligenes-faecalisen
dc.subjectSulfoxide reductaseen
dc.subject2fe-2s clusteren
dc.subjectOxidationen
dc.subjectEnzymeen
dc.subjectCytochromesen
dc.subjectMutagenesisen
dc.subjectQD Chemistryen
dc.subject.lccQDen
dc.titleThe respiratory arsenite oxidase : structure and the role of residues surrounding the rieske clusteren
dc.typeJournal articleen
dc.contributor.sponsorBBSRCen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doi10.1371/journal.pone.0072535
dc.description.statusPeer revieweden
dc.identifier.grantnumberBBS/B/14426en


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