The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster
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 detoxific...
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| Veröffentlicht in: | PloS one 2013-08, Vol.8 (8), p.e72535 |
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| creator | Warelow, Thomas P Oke, Muse Schoepp-Cothenet, Barbara Dahl, Jan U Bruselat, Nicole Sivalingam, Ganesh N Leimkühler, Silke Thalassinos, Konstantinos Kappler, Ulrike Naismith, James H Santini, Joanne M |
| description | 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 α subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small β 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. |
| doi_str_mv | 10.1371/journal.pone.0072535 |
| format | Article |
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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 α subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small β 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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0072535</identifier><identifier>PMID: 24023621</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Aerobiosis ; Alcaligenes ; Alcaligenes faecalis ; Alcaligenes faecalis - enzymology ; Alphaproteobacteria - enzymology ; Arsenates ; Arsenite ; Biochemistry ; Bioenergetics ; Biology ; Carbon ; Clusters ; Crystal structure ; Crystallography ; Cytochrome ; Cytochrome bc1 ; Detoxification ; Disulfides ; E coli ; Electrode potentials ; Electron paramagnetic resonance ; Electron Spin Resonance Spectroscopy ; Electron Transport Complex III - chemistry ; Electron Transport Complex III - metabolism ; Electrophoresis, Polyacrylamide Gel ; Enzymes ; Escherichia coli - metabolism ; Guanine ; Ligands ; Models, Molecular ; Molecular biology ; Molybdenum ; Molybdenum - metabolism ; Molybdopterin ; Mutagenesis ; Mutant Proteins - chemistry ; Mutant Proteins - metabolism ; Mutation - genetics ; Oxidase ; Oxidation ; Oxidation-Reduction ; Oxidoreductases - chemistry ; Oxidoreductases - isolation & purification ; Oxidoreductases - metabolism ; Protein Multimerization ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Redox potential ; Redox properties ; Rhodobacter sphaeroides ; Serine ; Site-directed mutagenesis ; Stability ; Structure-Activity Relationship ; Threonine</subject><ispartof>PloS one, 2013-08, Vol.8 (8), p.e72535</ispartof><rights>2013 Warelow et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Warelow et al 2013 Warelow et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-325ebe92985b1f75ebafefbe951354b006d237b694a5cd7243947f52a1e389353</citedby><cites>FETCH-LOGICAL-c526t-325ebe92985b1f75ebafefbe951354b006d237b694a5cd7243947f52a1e389353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3758308/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3758308/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24023621$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Soares, Claudio M.</contributor><creatorcontrib>Warelow, Thomas P</creatorcontrib><creatorcontrib>Oke, Muse</creatorcontrib><creatorcontrib>Schoepp-Cothenet, Barbara</creatorcontrib><creatorcontrib>Dahl, Jan U</creatorcontrib><creatorcontrib>Bruselat, Nicole</creatorcontrib><creatorcontrib>Sivalingam, Ganesh N</creatorcontrib><creatorcontrib>Leimkühler, Silke</creatorcontrib><creatorcontrib>Thalassinos, Konstantinos</creatorcontrib><creatorcontrib>Kappler, Ulrike</creatorcontrib><creatorcontrib>Naismith, James H</creatorcontrib><creatorcontrib>Santini, Joanne M</creatorcontrib><title>The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>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 α subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small β 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.</description><subject>Aerobiosis</subject><subject>Alcaligenes</subject><subject>Alcaligenes faecalis</subject><subject>Alcaligenes faecalis - enzymology</subject><subject>Alphaproteobacteria - enzymology</subject><subject>Arsenates</subject><subject>Arsenite</subject><subject>Biochemistry</subject><subject>Bioenergetics</subject><subject>Biology</subject><subject>Carbon</subject><subject>Clusters</subject><subject>Crystal structure</subject><subject>Crystallography</subject><subject>Cytochrome</subject><subject>Cytochrome bc1</subject><subject>Detoxification</subject><subject>Disulfides</subject><subject>E coli</subject><subject>Electrode potentials</subject><subject>Electron paramagnetic resonance</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Electron Transport Complex III - chemistry</subject><subject>Electron Transport Complex III - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes</subject><subject>Escherichia coli - metabolism</subject><subject>Guanine</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular biology</subject><subject>Molybdenum</subject><subject>Molybdenum - metabolism</subject><subject>Molybdopterin</subject><subject>Mutagenesis</subject><subject>Mutant Proteins - chemistry</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutation - genetics</subject><subject>Oxidase</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Oxidoreductases - metabolism</subject><subject>Protein Multimerization</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Redox potential</subject><subject>Redox properties</subject><subject>Rhodobacter sphaeroides</subject><subject>Serine</subject><subject>Site-directed mutagenesis</subject><subject>Stability</subject><subject>Structure-Activity 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Ulrike</au><au>Naismith, James H</au><au>Santini, Joanne M</au><au>Soares, Claudio M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-08-30</date><risdate>2013</risdate><volume>8</volume><issue>8</issue><spage>e72535</spage><pages>e72535-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><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 α subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small β 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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24023621</pmid><doi>10.1371/journal.pone.0072535</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2013-08, Vol.8 (8), p.e72535 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1428934476 |
| source | MEDLINE; Public Library of Science (PLoS) Journals Open Access; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Aerobiosis Alcaligenes Alcaligenes faecalis Alcaligenes faecalis - enzymology Alphaproteobacteria - enzymology Arsenates Arsenite Biochemistry Bioenergetics Biology Carbon Clusters Crystal structure Crystallography Cytochrome Cytochrome bc1 Detoxification Disulfides E coli Electrode potentials Electron paramagnetic resonance Electron Spin Resonance Spectroscopy Electron Transport Complex III - chemistry Electron Transport Complex III - metabolism Electrophoresis, Polyacrylamide Gel Enzymes Escherichia coli - metabolism Guanine Ligands Models, Molecular Molecular biology Molybdenum Molybdenum - metabolism Molybdopterin Mutagenesis Mutant Proteins - chemistry Mutant Proteins - metabolism Mutation - genetics Oxidase Oxidation Oxidation-Reduction Oxidoreductases - chemistry Oxidoreductases - isolation & purification Oxidoreductases - metabolism Protein Multimerization Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Redox potential Redox properties Rhodobacter sphaeroides Serine Site-directed mutagenesis Stability Structure-Activity Relationship Threonine |
| title | The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster |
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