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The respiratory arsenite oxidase : structure and the role of residues surrounding the rieske cluster

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Date
30/08/2013
Author
Warelow, Thomas P.
Oke, Muse
Schoepp-Cothenet, Barbara
Dahl, Jan U.
Bruselat, Nicole
Sivalingam, Ganesh N.
Leimkuehler, Silke
Thalassinos, Konstantinos
Kappler, Ulrike
Naismith, James H.
Santini, Joanne M.
Funder
BBSRC
Grant ID
BBS/B/14426
Keywords
Iron-sulfur protein
Escherichia-coli
Bc(1) complex
Alcaligenes-faecalis
Sulfoxide reductase
2fe-2s cluster
Oxidation
Enzyme
Cytochromes
Mutagenesis
QD Chemistry
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Abstract
The 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.
Citation
Warelow , 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.0072535
Publication
PLoS One
Status
Peer reviewed
DOI
https://doi.org/10.1371/journal.pone.0072535
ISSN
1932-6203
Type
Journal article
Rights
© 2013 Warelow et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description
Structural work was supported by grants from The Scottish Funding Council [grant number SULSA (to JHN)] and BBSRC [grant number BB/S/B14450 (to JHN).
Collections
  • University of St Andrews Research
URI
http://hdl.handle.net/10023/4693

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