Iron redox pathway revealed in ferritin via electron transfer analysis
Ferritin protein is involved in biological tissues in the storage and management of iron - an essential micro-nutrient in the majority of living systems. While there are extensive studies on iron-loaded ferritin, its functionality in iron delivery is not completely clear. Here, for the first time, d...
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| Veröffentlicht in: | Scientific reports 2020-03, Vol.10 (1), p.4033-4033, Article 4033 |
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| description | Ferritin protein is involved in biological tissues in the storage and management of iron - an essential micro-nutrient in the majority of living systems. While there are extensive studies on iron-loaded ferritin, its functionality in iron delivery is not completely clear. Here, for the first time, differential pulse voltammetry (DPV) has been successfully adapted to address the challenge of resolving a cascade of fast and co-occurring redox steps in enzymatic systems such as ferritin. Using DPV, comparative analysis of ferritins from two evolutionary-distant organisms has allowed us to propose a stepwise resolution for the complex mix of concurrent redox steps that is inherent to ferritins and to fine-tune the structure-function relationship of each redox step. Indeed, the cyclic conversion between Fe
3+
and Fe
2+
as well as the different oxidative steps of the various ferroxidase centers already known in ferritins were successfully discriminated, bringing new evidence that both the 3-fold and 4-fold channels can be functional in ferritin. |
| doi_str_mv | 10.1038/s41598-020-60640-z |
| format | Article |
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3+
and Fe
2+
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3+
and Fe
2+
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De Meulenaere, Evelien ; Deheyn, Dimitri D. ; Bandaru, Prabhakar R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-70fcbac22d59f027423920072cf2fdb7fc98b87ef34dd2a9fd9fab68c8da69803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>631/1647/2196</topic><topic>631/45/56</topic><topic>639/638/161</topic><topic>Binding sites</topic><topic>Comparative analysis</topic><topic>Crystal structure</topic><topic>Electron transfer</topic><topic>Enzyme kinetics</topic><topic>Ferritin</topic><topic>Ferroxidase</topic><topic>Humanities and Social Sciences</topic><topic>Iron</topic><topic>multidisciplinary</topic><topic>Mutation</topic><topic>Oxidation</topic><topic>Proteins</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Structure-function relationships</topic><topic>Voltammetry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Peng</creatorcontrib><creatorcontrib>De Meulenaere, Evelien</creatorcontrib><creatorcontrib>Deheyn, Dimitri D.</creatorcontrib><creatorcontrib>Bandaru, Prabhakar R.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health Medical collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>ProQuest Biological Science Journals</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Peng</au><au>De Meulenaere, Evelien</au><au>Deheyn, Dimitri D.</au><au>Bandaru, Prabhakar R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Iron redox pathway revealed in ferritin via electron transfer analysis</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2020-03-04</date><risdate>2020</risdate><volume>10</volume><issue>1</issue><spage>4033</spage><epage>4033</epage><pages>4033-4033</pages><artnum>4033</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Ferritin protein is involved in biological tissues in the storage and management of iron - an essential micro-nutrient in the majority of living systems. While there are extensive studies on iron-loaded ferritin, its functionality in iron delivery is not completely clear. Here, for the first time, differential pulse voltammetry (DPV) has been successfully adapted to address the challenge of resolving a cascade of fast and co-occurring redox steps in enzymatic systems such as ferritin. Using DPV, comparative analysis of ferritins from two evolutionary-distant organisms has allowed us to propose a stepwise resolution for the complex mix of concurrent redox steps that is inherent to ferritins and to fine-tune the structure-function relationship of each redox step. Indeed, the cyclic conversion between Fe
3+
and Fe
2+
as well as the different oxidative steps of the various ferroxidase centers already known in ferritins were successfully discriminated, bringing new evidence that both the 3-fold and 4-fold channels can be functional in ferritin.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>32132578</pmid><doi>10.1038/s41598-020-60640-z</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/1647/2196 631/45/56 639/638/161 Binding sites Comparative analysis Crystal structure Electron transfer Enzyme kinetics Ferritin Ferroxidase Humanities and Social Sciences Iron multidisciplinary Mutation Oxidation Proteins Science Science (multidisciplinary) Structure-function relationships Voltammetry |
| title | Iron redox pathway revealed in ferritin via electron transfer analysis |
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