Cluster and fold stability of E. coli ISC-type ferredoxin
Iron-sulfur clusters are essential protein prosthetic groups that provide their redox potential to several different metabolic pathways. Formation of iron-sulfur clusters is assisted by a specialised machine that comprises, among other proteins, a ferredoxin. As a first step to elucidate the precise...
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| Veröffentlicht in: | PloS one 2013-11, Vol.8 (11), p.e78948 |
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| creator | Yan, Robert Adinolfi, Salvatore Iannuzzi, Clara Kelly, Geoff Oregioni, Alain Martin, Stephen Pastore, Annalisa |
| description | Iron-sulfur clusters are essential protein prosthetic groups that provide their redox potential to several different metabolic pathways. Formation of iron-sulfur clusters is assisted by a specialised machine that comprises, among other proteins, a ferredoxin. As a first step to elucidate the precise role of this protein in cluster assembly, we have studied the factors governing the stability and the dynamic properties of E. coli ferredoxin using different spectroscopic techniques. The cluster-loaded protein is monomeric and well structured with a flexible C-terminus but is highly oxygen sensitive so that it readily loses the cluster leading to an irreversible unfolding under aerobic conditions. This process is slowed down by reducing conditions and high ionic strengths. NMR relaxation experiments on the cluster-loaded protein also show that, once the cluster is in place, the protein forms a globular and relatively rigid domain. These data indicate that the presence of the iron-sulfur cluster is the switch between a functional and a non-functional state. |
| doi_str_mv | 10.1371/journal.pone.0078948 |
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Formation of iron-sulfur clusters is assisted by a specialised machine that comprises, among other proteins, a ferredoxin. As a first step to elucidate the precise role of this protein in cluster assembly, we have studied the factors governing the stability and the dynamic properties of E. coli ferredoxin using different spectroscopic techniques. The cluster-loaded protein is monomeric and well structured with a flexible C-terminus but is highly oxygen sensitive so that it readily loses the cluster leading to an irreversible unfolding under aerobic conditions. This process is slowed down by reducing conditions and high ionic strengths. NMR relaxation experiments on the cluster-loaded protein also show that, once the cluster is in place, the protein forms a globular and relatively rigid domain. These data indicate that the presence of the iron-sulfur cluster is the switch between a functional and a non-functional state.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0078948</identifier><identifier>PMID: 24265733</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Aerobic conditions ; Biochemistry ; Biosynthesis ; C-Terminus ; Cloning ; Clusters ; Councils ; Deoxyribonucleic acid ; DNA ; Dose-Response Relationship, Drug ; Dynamic stability ; E coli ; Enzymes ; Escherichia coli ; Ferredoxin ; Ferredoxins - chemistry ; Ferredoxins - metabolism ; Gene expression ; Iron ; Iron - chemistry ; Medical research ; Metabolic pathways ; Models, Molecular ; Molecular structure ; NMR ; Nuclear magnetic resonance ; Oxygen ; Phosphines - pharmacology ; Prostheses ; Prosthetic groups ; Protein Conformation - drug effects ; Protein folding ; Protein Folding - drug effects ; Protein Stability - drug effects ; Proteins ; Redox potential ; Sodium Chloride - pharmacology ; Sulfur ; Sulfur - chemistry ; Sulfur compounds ; Temperature</subject><ispartof>PloS one, 2013-11, Vol.8 (11), p.e78948</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Yan et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/3.0/ (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 Yan et al 2013 Yan et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-d6bda55b3a4b0f446eb133d5d3ec855fceb0283bb921679be7fecc394d1ee6fb3</citedby><cites>FETCH-LOGICAL-c692t-d6bda55b3a4b0f446eb133d5d3ec855fceb0283bb921679be7fecc394d1ee6fb3</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/PMC3827102/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3827102/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2929,23871,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24265733$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Cavalli, Andrea</contributor><creatorcontrib>Yan, Robert</creatorcontrib><creatorcontrib>Adinolfi, Salvatore</creatorcontrib><creatorcontrib>Iannuzzi, Clara</creatorcontrib><creatorcontrib>Kelly, Geoff</creatorcontrib><creatorcontrib>Oregioni, Alain</creatorcontrib><creatorcontrib>Martin, Stephen</creatorcontrib><creatorcontrib>Pastore, Annalisa</creatorcontrib><title>Cluster and fold stability of E. coli ISC-type ferredoxin</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Iron-sulfur clusters are essential protein prosthetic groups that provide their redox potential to several different metabolic pathways. Formation of iron-sulfur clusters is assisted by a specialised machine that comprises, among other proteins, a ferredoxin. As a first step to elucidate the precise role of this protein in cluster assembly, we have studied the factors governing the stability and the dynamic properties of E. coli ferredoxin using different spectroscopic techniques. The cluster-loaded protein is monomeric and well structured with a flexible C-terminus but is highly oxygen sensitive so that it readily loses the cluster leading to an irreversible unfolding under aerobic conditions. This process is slowed down by reducing conditions and high ionic strengths. NMR relaxation experiments on the cluster-loaded protein also show that, once the cluster is in place, the protein forms a globular and relatively rigid domain. These data indicate that the presence of the iron-sulfur cluster is the switch between a functional and a non-functional state.</description><subject>Aerobic conditions</subject><subject>Biochemistry</subject><subject>Biosynthesis</subject><subject>C-Terminus</subject><subject>Cloning</subject><subject>Clusters</subject><subject>Councils</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Dose-Response Relationship, Drug</subject><subject>Dynamic stability</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Ferredoxin</subject><subject>Ferredoxins - chemistry</subject><subject>Ferredoxins - metabolism</subject><subject>Gene expression</subject><subject>Iron</subject><subject>Iron - chemistry</subject><subject>Medical research</subject><subject>Metabolic pathways</subject><subject>Models, Molecular</subject><subject>Molecular structure</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Oxygen</subject><subject>Phosphines - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yan, Robert</au><au>Adinolfi, Salvatore</au><au>Iannuzzi, Clara</au><au>Kelly, Geoff</au><au>Oregioni, Alain</au><au>Martin, Stephen</au><au>Pastore, Annalisa</au><au>Cavalli, Andrea</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cluster and fold stability of E. coli ISC-type ferredoxin</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-11-12</date><risdate>2013</risdate><volume>8</volume><issue>11</issue><spage>e78948</spage><pages>e78948-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Iron-sulfur clusters are essential protein prosthetic groups that provide their redox potential to several different metabolic pathways. Formation of iron-sulfur clusters is assisted by a specialised machine that comprises, among other proteins, a ferredoxin. As a first step to elucidate the precise role of this protein in cluster assembly, we have studied the factors governing the stability and the dynamic properties of E. coli ferredoxin using different spectroscopic techniques. The cluster-loaded protein is monomeric and well structured with a flexible C-terminus but is highly oxygen sensitive so that it readily loses the cluster leading to an irreversible unfolding under aerobic conditions. This process is slowed down by reducing conditions and high ionic strengths. NMR relaxation experiments on the cluster-loaded protein also show that, once the cluster is in place, the protein forms a globular and relatively rigid domain. These data indicate that the presence of the iron-sulfur cluster is the switch between a functional and a non-functional state.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24265733</pmid><doi>10.1371/journal.pone.0078948</doi><tpages>e78948</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Aerobic conditions Biochemistry Biosynthesis C-Terminus Cloning Clusters Councils Deoxyribonucleic acid DNA Dose-Response Relationship, Drug Dynamic stability E coli Enzymes Escherichia coli Ferredoxin Ferredoxins - chemistry Ferredoxins - metabolism Gene expression Iron Iron - chemistry Medical research Metabolic pathways Models, Molecular Molecular structure NMR Nuclear magnetic resonance Oxygen Phosphines - pharmacology Prostheses Prosthetic groups Protein Conformation - drug effects Protein folding Protein Folding - drug effects Protein Stability - drug effects Proteins Redox potential Sodium Chloride - pharmacology Sulfur Sulfur - chemistry Sulfur compounds Temperature |
| title | Cluster and fold stability of E. coli ISC-type ferredoxin |
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