Characterization of Glutaredoxin Fe-S Cluster-Binding Interactions Using Circular Dichroism Spectroscopy.
Identifieur interne : 000284 ( Main/Exploration ); précédent : 000283; suivant : 000285Characterization of Glutaredoxin Fe-S Cluster-Binding Interactions Using Circular Dichroism Spectroscopy.
Auteurs : Angela-Nadia Albetel [États-Unis] ; Caryn E. Outten [États-Unis]Source :
- Methods in enzymology [ 1557-7988 ] ; 2018.
Descripteurs français
- KwdFr :
- Cartes d'interactions protéiques (MeSH), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Dichroïsme circulaire (méthodes), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Liaison aux protéines (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines et peptides de signalisation intracellulaire (composition chimique), Protéines et peptides de signalisation intracellulaire (métabolisme), Saccharomyces cerevisiae (composition chimique), Saccharomyces cerevisiae (métabolisme), Thermodynamique (MeSH).
- MESH :
- composition chimique : Ferrosulfoprotéines, Glutarédoxines, Oxidoreductases, Protéines de Saccharomyces cerevisiae, Protéines et peptides de signalisation intracellulaire, Saccharomyces cerevisiae.
- métabolisme : Ferrosulfoprotéines, Glutarédoxines, Oxidoreductases, Protéines de Saccharomyces cerevisiae, Protéines et peptides de signalisation intracellulaire, Saccharomyces cerevisiae.
- méthodes : Dichroïsme circulaire.
- Cartes d'interactions protéiques, Cinétique, Concentration en ions d'hydrogène, Liaison aux protéines, Thermodynamique.
English descriptors
- KwdEn :
- Circular Dichroism (methods), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Hydrogen-Ion Concentration (MeSH), Intracellular Signaling Peptides and Proteins (chemistry), Intracellular Signaling Peptides and Proteins (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Kinetics (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Protein Binding (MeSH), Protein Interaction Maps (MeSH), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Glutaredoxins, Intracellular Signaling Peptides and Proteins, Iron-Sulfur Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glutaredoxins, Intracellular Signaling Peptides and Proteins, Iron-Sulfur Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemistry : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- methods : Circular Dichroism.
- Hydrogen-Ion Concentration, Kinetics, Protein Binding, Protein Interaction Maps, Thermodynamics.
Abstract
Monothiol glutaredoxins (Grxs) with a conserved Cys-Gly-Phe-Ser (CGFS) active site are iron-sulfur (Fe-S) cluster-binding proteins that interact with a variety of partner proteins and perform crucial roles in iron metabolism including Fe-S cluster transfer, Fe-S cluster repair, and iron signaling. Various analytical and spectroscopic methods are currently being used to monitor and characterize glutaredoxin Fe-S cluster-dependent interactions at the molecular level. The electronic, magnetic, and vibrational properties of the protein-bound Fe-S cluster provide a convenient handle to probe the structure, function, and coordination chemistry of Grx complexes. However, some limitations arise from sample preparation requirements, complexity of individual techniques, or the necessity for combining multiple methods in order to achieve a complete investigation. In this chapter, we focus on the use of UV-visible circular dichroism spectroscopy as a fast and simple initial approach for investigating glutaredoxin Fe-S cluster-dependent interactions.
DOI: 10.1016/bs.mie.2017.11.003
PubMed: 29746245
PubMed Central: PMC6427907
Affiliations:
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Various analytical and spectroscopic methods are currently being used to monitor and characterize glutaredoxin Fe-S cluster-dependent interactions at the molecular level. The electronic, magnetic, and vibrational properties of the protein-bound Fe-S cluster provide a convenient handle to probe the structure, function, and coordination chemistry of Grx complexes. However, some limitations arise from sample preparation requirements, complexity of individual techniques, or the necessity for combining multiple methods in order to achieve a complete investigation. In this chapter, we focus on the use of UV-visible circular dichroism spectroscopy as a fast and simple initial approach for investigating glutaredoxin Fe-S cluster-dependent interactions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29746245</PMID><DateCompleted><Year>2019</Year><Month>02</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7988</ISSN><JournalIssue CitedMedium="Internet"><Volume>599</Volume><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>Methods in enzymology</Title><ISOAbbreviation>Methods Enzymol</ISOAbbreviation></Journal><ArticleTitle>Characterization of Glutaredoxin Fe-S Cluster-Binding Interactions Using Circular Dichroism Spectroscopy.</ArticleTitle><Pagination><MedlinePgn>327-353</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0076-6879(17)30341-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/bs.mie.2017.11.003</ELocationID><Abstract><AbstractText>Monothiol glutaredoxins (Grxs) with a conserved Cys-Gly-Phe-Ser (CGFS) active site are iron-sulfur (Fe-S) cluster-binding proteins that interact with a variety of partner proteins and perform crucial roles in iron metabolism including Fe-S cluster transfer, Fe-S cluster repair, and iron signaling. Various analytical and spectroscopic methods are currently being used to monitor and characterize glutaredoxin Fe-S cluster-dependent interactions at the molecular level. The electronic, magnetic, and vibrational properties of the protein-bound Fe-S cluster provide a convenient handle to probe the structure, function, and coordination chemistry of Grx complexes. However, some limitations arise from sample preparation requirements, complexity of individual techniques, or the necessity for combining multiple methods in order to achieve a complete investigation. In this chapter, we focus on the use of UV-visible circular dichroism spectroscopy as a fast and simple initial approach for investigating glutaredoxin Fe-S cluster-dependent interactions.</AbstractText><CopyrightInformation>© 2018 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Albetel</LastName><ForeName>Angela-Nadia</ForeName><Initials>AN</Initials><AffiliationInfo><Affiliation>University of South Carolina, Columbia, SC, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Outten</LastName><ForeName>Caryn E</ForeName><Initials>CE</Initials><AffiliationInfo><Affiliation>University of South Carolina, Columbia, SC, United States. 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IdType="pubmed">8910356</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Sud</li></region><settlement><li>Columbia (Caroline du Sud)</li></settlement><orgName><li>Université de Caroline du Sud</li></orgName></list><tree><country name="États-Unis"><region name="Caroline du Sud"><name sortKey="Albetel, Angela Nadia" sort="Albetel, Angela Nadia" uniqKey="Albetel A" first="Angela-Nadia" last="Albetel">Angela-Nadia Albetel</name></region><name sortKey="Outten, Caryn E" sort="Outten, Caryn E" uniqKey="Outten C" first="Caryn E" last="Outten">Caryn E. 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