IronSulferCluV1, Main, Exploration, bibRecord, 000199

The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.

Identifieur interne : 000199 ( Main/Exploration ); précédent : 000198; suivant : 000200

The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.

Auteurs : Aaron T. Smith [États-Unis] ; Richard O. Linkous [États-Unis] ; Nathan J. Max [États-Unis] ; Alexandrea E. Sestok [États-Unis] ; Veronika A. Szalai [États-Unis] ; Kelly N. Chac N [États-Unis]

Source :

Biochemistry [ 1520-4995 ] ; 2019.

RBID : pubmed:31713418

Descripteurs français

English descriptors

KwdEn :
- Catalytic Domain (MeSH), Electron Spin Resonance Spectroscopy (MeSH), Escherichia coli (chemistry), Escherichia coli (genetics), Escherichia coli (metabolism), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (genetics), Escherichia coli Proteins (metabolism), Iron (chemistry), Iron (metabolism), Iron-Binding Proteins (chemistry), Iron-Binding Proteins (genetics), Iron-Binding Proteins (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Kinetics (MeSH), Oxidation-Reduction (MeSH), Oxygen (chemistry), Oxygen (metabolism), Repressor Proteins (chemistry), Repressor Proteins (genetics), Repressor Proteins (metabolism), Sulfur (chemistry), Sulfur (metabolism).
MESH :
- chemical , chemistry : Escherichia coli Proteins, Iron, Iron-Binding Proteins, Iron-Sulfur Proteins, Oxygen, Repressor Proteins, Sulfur.
- chemistry : Escherichia coli.
- genetics : Escherichia coli, Escherichia coli Proteins, Iron-Binding Proteins, Iron-Sulfur Proteins, Repressor Proteins.
- metabolism : Escherichia coli, Escherichia coli Proteins, Iron, Iron-Binding Proteins, Iron-Sulfur Proteins, Oxygen, Repressor Proteins, Sulfur.
- Catalytic Domain, Electron Spin Resonance Spectroscopy, Kinetics, Oxidation-Reduction.

Abstract

The acquisition of iron is essential to establishing virulence among most pathogens. Under acidic and/or anaerobic conditions, most bacteria utilize the widely distributed ferrous iron (Fe²⁺) uptake (Feo) system to import metabolically-required iron. The Feo system is inadequately understood at the atomic, molecular, and mechanistic levels, but we do know it is composed of a main membrane component (FeoB) essential for iron translocation, as well as two small, cytosolic proteins (FeoA and FeoC) hypothesized to function as accessories to this process. FeoC has many hypothetical functions, including that of an iron-responsive transcriptional regulator. Here, we demonstrate for the first time that Escherichia coli FeoC (EcFeoC) binds an [Fe-S] cluster. Using electronic absorption, X-ray absorption, and electron paramagnetic resonance spectroscopies, we extensively characterize the nature of this cluster. Under strictly anaerobic conditions after chemical reconstitution, we demonstrate that EcFeoC binds a redox-active [4Fe-4S]^2+/+ cluster that is rapidly oxygen-sensitive and decays to a [2Fe-2S]²⁺ cluster (t_1/2 ≈ 20 s), similar to the [Fe-S] cluster in the fumarate and nitrate reductase (FNR) transcriptional regulator. We further show that this behavior is nearly identical to the homologous K. pneumoniae FeoC, suggesting a redox-active, oxygen-sensitive [4Fe-4S]²⁺ cofactor is a general phenomenon of cluster-binding FeoCs. Finally, in contrast to FNR, we show that the [4Fe-4S]²⁺ cluster binding to FeoC is associated with modest conformational changes of the polypeptide, but not protein dimerization. We thus posit a working hypothesis in which the cluster-binding FeoCs may function as oxygen-sensitive iron sensors that fine-tune pathogenic ferrous iron acquisition.

DOI: 10.1021/acs.biochem.9b00745
PubMed: 31713418
PubMed Central: PMC6904521

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<author><name sortKey="Linkous, Richard O" sort="Linkous, Richard O" uniqKey="Linkous R" first="Richard O" last="Linkous">Richard O. Linkous</name>
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<country xml:lang="fr">États-Unis</country>
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<series><title level="j">Biochemistry</title>
<idno type="eISSN">1520-4995</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalytic Domain (MeSH)</term>
<term>Electron Spin Resonance Spectroscopy (MeSH)</term>
<term>Escherichia coli (chemistry)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Escherichia coli Proteins (chemistry)</term>
<term>Escherichia coli Proteins (genetics)</term>
<term>Escherichia coli Proteins (metabolism)</term>
<term>Iron (chemistry)</term>
<term>Iron (metabolism)</term>
<term>Iron-Binding Proteins (chemistry)</term>
<term>Iron-Binding Proteins (genetics)</term>
<term>Iron-Binding Proteins (metabolism)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxygen (chemistry)</term>
<term>Oxygen (metabolism)</term>
<term>Repressor Proteins (chemistry)</term>
<term>Repressor Proteins (genetics)</term>
<term>Repressor Proteins (metabolism)</term>
<term>Sulfur (chemistry)</term>
<term>Sulfur (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Escherichia coli (composition chimique)</term>
<term>Escherichia coli (génétique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Fer (composition chimique)</term>
<term>Fer (métabolisme)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Oxygène (composition chimique)</term>
<term>Oxygène (métabolisme)</term>
<term>Protéines Escherichia coli (composition chimique)</term>
<term>Protéines Escherichia coli (génétique)</term>
<term>Protéines Escherichia coli (métabolisme)</term>
<term>Protéines de liaison au fer (composition chimique)</term>
<term>Protéines de liaison au fer (génétique)</term>
<term>Protéines de liaison au fer (métabolisme)</term>
<term>Protéines de répression (composition chimique)</term>
<term>Protéines de répression (génétique)</term>
<term>Protéines de répression (métabolisme)</term>
<term>Soufre (composition chimique)</term>
<term>Soufre (métabolisme)</term>
<term>Spectroscopie de résonance de spin électronique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Escherichia coli Proteins</term>
<term>Iron</term>
<term>Iron-Binding Proteins</term>
<term>Iron-Sulfur Proteins</term>
<term>Oxygen</term>
<term>Repressor Proteins</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Escherichia coli</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Escherichia coli</term>
<term>Fer</term>
<term>Ferrosulfoprotéines</term>
<term>Oxygène</term>
<term>Protéines Escherichia coli</term>
<term>Protéines de liaison au fer</term>
<term>Protéines de répression</term>
<term>Soufre</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
<term>Escherichia coli Proteins</term>
<term>Iron-Binding Proteins</term>
<term>Iron-Sulfur Proteins</term>
<term>Repressor Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term>
<term>Ferrosulfoprotéines</term>
<term>Protéines Escherichia coli</term>
<term>Protéines de liaison au fer</term>
<term>Protéines de répression</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term>
<term>Escherichia coli Proteins</term>
<term>Iron</term>
<term>Iron-Binding Proteins</term>
<term>Iron-Sulfur Proteins</term>
<term>Oxygen</term>
<term>Repressor Proteins</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term>
<term>Fer</term>
<term>Ferrosulfoprotéines</term>
<term>Oxygène</term>
<term>Protéines Escherichia coli</term>
<term>Protéines de liaison au fer</term>
<term>Protéines de répression</term>
<term>Soufre</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term>
<term>Electron Spin Resonance Spectroscopy</term>
<term>Kinetics</term>
<term>Oxidation-Reduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term>
<term>Domaine catalytique</term>
<term>Oxydoréduction</term>
<term>Spectroscopie de résonance de spin électronique</term>
</keywords>
</textClass>
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<front><div type="abstract" xml:lang="en">The acquisition of iron is essential to establishing virulence among most pathogens. Under acidic and/or anaerobic conditions, most bacteria utilize the widely distributed ferrous iron (Fe<sup>2+</sup>
) uptake (Feo) system to import metabolically-required iron. The Feo system is inadequately understood at the atomic, molecular, and mechanistic levels, but we do know it is composed of a main membrane component (FeoB) essential for iron translocation, as well as two small, cytosolic proteins (FeoA and FeoC) hypothesized to function as accessories to this process. FeoC has many hypothetical functions, including that of an iron-responsive transcriptional regulator. Here, we demonstrate for the first time that <i>Escherichia coli</i>
 FeoC (<i>Ec</i>
FeoC) binds an [Fe-S] cluster. Using electronic absorption, X-ray absorption, and electron paramagnetic resonance spectroscopies, we extensively characterize the nature of this cluster. Under strictly anaerobic conditions after chemical reconstitution, we demonstrate that <i>Ec</i>
FeoC binds a redox-active [4Fe-4S]<sup>2+/+</sup>
 cluster that is rapidly oxygen-sensitive and decays to a [2Fe-2S]<sup>2+</sup>
 cluster (<i>t</i>
<sub>1/2</sub>
 ≈ 20 s), similar to the [Fe-S] cluster in the fumarate and nitrate reductase (FNR) transcriptional regulator. We further show that this behavior is nearly identical to the homologous <i>K. pneumoniae</i>
 FeoC, suggesting a redox-active, oxygen-sensitive [4Fe-4S]<sup>2+</sup>
 cofactor is a general phenomenon of cluster-binding FeoCs. Finally, in contrast to FNR, we show that the [4Fe-4S]<sup>2+</sup>
 cluster binding to FeoC is associated with modest conformational changes of the polypeptide, but not protein dimerization. We thus posit a working hypothesis in which the cluster-binding FeoCs may function as oxygen-sensitive iron sensors that fine-tune pathogenic ferrous iron acquisition.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31713418</PMID>
<DateCompleted><Year>2020</Year>
<Month>06</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>08</Month>
<Day>27</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>58</Volume>
<Issue>49</Issue>
<PubDate><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</PubDate>
</JournalIssue>
<Title>Biochemistry</Title>
<ISOAbbreviation>Biochemistry</ISOAbbreviation>
</Journal>
<ArticleTitle>The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.</ArticleTitle>
<Pagination><MedlinePgn>4935-4949</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.9b00745</ELocationID>
<Abstract><AbstractText>The acquisition of iron is essential to establishing virulence among most pathogens. Under acidic and/or anaerobic conditions, most bacteria utilize the widely distributed ferrous iron (Fe<sup>2+</sup>
) uptake (Feo) system to import metabolically-required iron. The Feo system is inadequately understood at the atomic, molecular, and mechanistic levels, but we do know it is composed of a main membrane component (FeoB) essential for iron translocation, as well as two small, cytosolic proteins (FeoA and FeoC) hypothesized to function as accessories to this process. FeoC has many hypothetical functions, including that of an iron-responsive transcriptional regulator. Here, we demonstrate for the first time that <i>Escherichia coli</i>
 FeoC (<i>Ec</i>
FeoC) binds an [Fe-S] cluster. Using electronic absorption, X-ray absorption, and electron paramagnetic resonance spectroscopies, we extensively characterize the nature of this cluster. Under strictly anaerobic conditions after chemical reconstitution, we demonstrate that <i>Ec</i>
FeoC binds a redox-active [4Fe-4S]<sup>2+/+</sup>
 cluster that is rapidly oxygen-sensitive and decays to a [2Fe-2S]<sup>2+</sup>
 cluster (<i>t</i>
<sub>1/2</sub>
 ≈ 20 s), similar to the [Fe-S] cluster in the fumarate and nitrate reductase (FNR) transcriptional regulator. We further show that this behavior is nearly identical to the homologous <i>K. pneumoniae</i>
 FeoC, suggesting a redox-active, oxygen-sensitive [4Fe-4S]<sup>2+</sup>
 cofactor is a general phenomenon of cluster-binding FeoCs. Finally, in contrast to FNR, we show that the [4Fe-4S]<sup>2+</sup>
 cluster binding to FeoC is associated with modest conformational changes of the polypeptide, but not protein dimerization. We thus posit a working hypothesis in which the cluster-binding FeoCs may function as oxygen-sensitive iron sensors that fine-tune pathogenic ferrous iron acquisition.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Smith</LastName>
<ForeName>Aaron T</ForeName>
<Initials>AT</Initials>
<Identifier Source="ORCID">0000-0002-9332-8683</Identifier>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry , University of Maryland, Baltimore County , Baltimore , Maryland 21250 United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Linkous</LastName>
<ForeName>Richard O</ForeName>
<Initials>RO</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry , University of Maryland, Baltimore County , Baltimore , Maryland 21250 United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Max</LastName>
<ForeName>Nathan J</ForeName>
<Initials>NJ</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry , University of Maryland, Baltimore County , Baltimore , Maryland 21250 United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sestok</LastName>
<ForeName>Alexandrea E</ForeName>
<Initials>AE</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry , University of Maryland, Baltimore County , Baltimore , Maryland 21250 United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Szalai</LastName>
<ForeName>Veronika A</ForeName>
<Initials>VA</Initials>
<AffiliationInfo><Affiliation>Physical Measurement Laboratory , National Institute of Standards and Technology , Gaithersburg , Maryland 20899 , United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chacón</LastName>
<ForeName>Kelly N</ForeName>
<Initials>KN</Initials>
<Identifier Source="ORCID">0000-0003-1332-7283</Identifier>
<AffiliationInfo><Affiliation>Department of Chemistry , Reed College , Portland , Oregon 97202 , United States.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R35 GM133497</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32 GM066706</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>P41 GM103393</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>11</Month>
<Day>21</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Biochemistry</MedlineTA>
<NlmUniqueID>0370623</NlmUniqueID>
<ISSNLinking>0006-2960</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C000707998">FeoC protein, E coli</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D033862">Iron-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012097">Repressor Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>70FD1KFU70</RegistryNumber>
<NameOfSubstance UI="D013455">Sulfur</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>E1UOL152H7</RegistryNumber>
<NameOfSubstance UI="D007501">Iron</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>S88TT14065</RegistryNumber>
<NameOfSubstance UI="D010100">Oxygen</NameOfSubstance>
</Chemical>
</ChemicalList>
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   |texte=   The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.
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The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.

The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.

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