IronSulferCluV1, Main, Exploration, bibRecord, 000236

H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.

Identifieur interne : 000236 ( Main/Exploration ); précédent : 000235; suivant : 000237

H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.

Auteurs : Amanda S. Byer [États-Unis] ; Eric M. Shepard [États-Unis] ; Michael W. Ratzloff [États-Unis] ; Jeremiah N. Betz [États-Unis] ; Paul W. King [États-Unis] ; William E. Broderick [États-Unis] ; Joan B. Broderick [États-Unis]

Source :

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [ 1432-1327 ] ; 2019.

RBID : pubmed:31493152

Descripteurs français

English descriptors

KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Clostridium acetobutylicum (enzymology), Clostridium acetobutylicum (metabolism), Electron Spin Resonance Spectroscopy (MeSH), Hydrogenase (chemistry), Hydrogenase (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Protein Conformation (MeSH), S-Adenosylmethionine (chemistry), S-Adenosylmethionine (metabolism), Spectroscopy, Fourier Transform Infrared (MeSH).
MESH :
- chemical , chemistry : Bacterial Proteins, Hydrogenase, Iron-Sulfur Proteins, S-Adenosylmethionine.
- chemical , metabolism : Bacterial Proteins, Hydrogenase, Iron-Sulfur Proteins, S-Adenosylmethionine.
- enzymology : Clostridium acetobutylicum.
- metabolism : Clostridium acetobutylicum.
- Electron Spin Resonance Spectroscopy, Protein Conformation, Spectroscopy, Fourier Transform Infrared.

Abstract

[FeFe]-hydrogenase catalyzes the reversible reduction of protons to H₂ at a complex metallocofactor site, the H-cluster. Biosynthesis of this active-site H-cluster requires three maturation enzymes: the radical S-adenosylmethionine enzymes HydE and HydG synthesize the nonprotein ligands, while the GTPase HydF provides a scaffold for assembly of the 2Fe subcluster of the H-cluster ([2Fe]_H) prior to its transfer to hydrogenase. To delineate the assembly and delivery steps for the 2Fe precursor cluster coordinated to HydF ([2Fe]_F), we have heterologously expressed HydF in the presence of HydE alone (HydF^E) or HydG alone (HydF^G), and characterized the resulting purified HydF^E and HydF^G using UV-visible, EPR, and FTIR spectroscopies and biochemical assays. The iron-sulfur clusters on HydF are modified by co-expression with HydE or HydG, as evidenced by the changes in the visible, EPR, and FTIR spectral features. Further, biochemical assays show that HydF^E is capable of activating HydA^ΔEFG to a limited extent (~ 1% of WT) even though the normal source of CO and CN^- ligands of [2Fe]_H (HydG) was absent. Activation assays performed with HydF^G, in contrast, exhibit no ability to mature HydA^ΔEFG. It appears that in the case of HydF^E, trace diatomics from the cellular environment are incorporated into a [2Fe]_F-like precursor on HydF in the absence of HydG. We conclude that the product of HydE, presumably the dithiomethylamine ligand of [2Fe]_H, is absolutely essential to the activation process, while the diatomic products of HydG can be provided from alternate sources.

DOI: 10.1007/s00775-019-01709-7
PubMed: 31493152

Affiliations:

États-Unis

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

to stream Main, to step Corpus: 000243
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Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en">H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.</title>
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<series><title level="j">Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</title>
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<term>Bacterial Proteins (metabolism)</term>
<term>Clostridium acetobutylicum (enzymology)</term>
<term>Clostridium acetobutylicum (metabolism)</term>
<term>Electron Spin Resonance Spectroscopy (MeSH)</term>
<term>Hydrogenase (chemistry)</term>
<term>Hydrogenase (metabolism)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Protein Conformation (MeSH)</term>
<term>S-Adenosylmethionine (chemistry)</term>
<term>S-Adenosylmethionine (metabolism)</term>
<term>Spectroscopy, Fourier Transform Infrared (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Adémétionine (composition chimique)</term>
<term>Adémétionine (métabolisme)</term>
<term>Clostridium acetobutylicum (enzymologie)</term>
<term>Clostridium acetobutylicum (métabolisme)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Hydrogenase (composition chimique)</term>
<term>Hydrogenase (métabolisme)</term>
<term>Protéines bactériennes (composition chimique)</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Spectroscopie de résonance de spin électronique (MeSH)</term>
<term>Spectroscopie infrarouge à transformée de Fourier (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term>
<term>Hydrogenase</term>
<term>Iron-Sulfur Proteins</term>
<term>S-Adenosylmethionine</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term>
<term>Hydrogenase</term>
<term>Iron-Sulfur Proteins</term>
<term>S-Adenosylmethionine</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Adémétionine</term>
<term>Ferrosulfoprotéines</term>
<term>Hydrogenase</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Clostridium acetobutylicum</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Clostridium acetobutylicum</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Clostridium acetobutylicum</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adémétionine</term>
<term>Clostridium acetobutylicum</term>
<term>Ferrosulfoprotéines</term>
<term>Hydrogenase</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Electron Spin Resonance Spectroscopy</term>
<term>Protein Conformation</term>
<term>Spectroscopy, Fourier Transform Infrared</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term>
<term>Spectroscopie de résonance de spin électronique</term>
<term>Spectroscopie infrarouge à transformée de Fourier</term>
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<front><div type="abstract" xml:lang="en">[FeFe]-hydrogenase catalyzes the reversible reduction of protons to H<sub>2</sub>
 at a complex metallocofactor site, the H-cluster. Biosynthesis of this active-site H-cluster requires three maturation enzymes: the radical S-adenosylmethionine enzymes HydE and HydG synthesize the nonprotein ligands, while the GTPase HydF provides a scaffold for assembly of the 2Fe subcluster of the H-cluster ([2Fe]<sub>H</sub>
) prior to its transfer to hydrogenase. To delineate the assembly and delivery steps for the 2Fe precursor cluster coordinated to HydF ([2Fe]<sub>F</sub>
), we have heterologously expressed HydF in the presence of HydE alone (HydF<sup>E</sup>
) or HydG alone (HydF<sup>G</sup>
), and characterized the resulting purified HydF<sup>E</sup>
 and HydF<sup>G</sup>
 using UV-visible, EPR, and FTIR spectroscopies and biochemical assays. The iron-sulfur clusters on HydF are modified by co-expression with HydE or HydG, as evidenced by the changes in the visible, EPR, and FTIR spectral features. Further, biochemical assays show that HydF<sup>E</sup>
 is capable of activating HydA<sup>ΔEFG</sup>
 to a limited extent (~ 1% of WT) even though the normal source of CO and CN<sup>-</sup>
 ligands of [2Fe]<sub>H</sub>
 (HydG) was absent. Activation assays performed with HydF<sup>G</sup>
, in contrast, exhibit no ability to mature HydA<sup>ΔEFG</sup>
. It appears that in the case of HydF<sup>E</sup>
, trace diatomics from the cellular environment are incorporated into a [2Fe]<sub>F</sub>
-like precursor on HydF in the absence of HydG. We conclude that the product of HydE, presumably the dithiomethylamine ligand of [2Fe]<sub>H</sub>
, is absolutely essential to the activation process, while the diatomic products of HydG can be provided from alternate sources.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31493152</PMID>
<DateCompleted><Year>2020</Year>
<Month>07</Month>
<Day>13</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>07</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-1327</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>24</Volume>
<Issue>6</Issue>
<PubDate><Year>2019</Year>
<Month>09</Month>
</PubDate>
</JournalIssue>
<Title>Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</Title>
<ISOAbbreviation>J Biol Inorg Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.</ArticleTitle>
<Pagination><MedlinePgn>783-792</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1007/s00775-019-01709-7</ELocationID>
<Abstract><AbstractText>[FeFe]-hydrogenase catalyzes the reversible reduction of protons to H<sub>2</sub>
 at a complex metallocofactor site, the H-cluster. Biosynthesis of this active-site H-cluster requires three maturation enzymes: the radical S-adenosylmethionine enzymes HydE and HydG synthesize the nonprotein ligands, while the GTPase HydF provides a scaffold for assembly of the 2Fe subcluster of the H-cluster ([2Fe]<sub>H</sub>
) prior to its transfer to hydrogenase. To delineate the assembly and delivery steps for the 2Fe precursor cluster coordinated to HydF ([2Fe]<sub>F</sub>
), we have heterologously expressed HydF in the presence of HydE alone (HydF<sup>E</sup>
) or HydG alone (HydF<sup>G</sup>
), and characterized the resulting purified HydF<sup>E</sup>
 and HydF<sup>G</sup>
 using UV-visible, EPR, and FTIR spectroscopies and biochemical assays. The iron-sulfur clusters on HydF are modified by co-expression with HydE or HydG, as evidenced by the changes in the visible, EPR, and FTIR spectral features. Further, biochemical assays show that HydF<sup>E</sup>
 is capable of activating HydA<sup>ΔEFG</sup>
 to a limited extent (~ 1% of WT) even though the normal source of CO and CN<sup>-</sup>
 ligands of [2Fe]<sub>H</sub>
 (HydG) was absent. Activation assays performed with HydF<sup>G</sup>
, in contrast, exhibit no ability to mature HydA<sup>ΔEFG</sup>
. It appears that in the case of HydF<sup>E</sup>
, trace diatomics from the cellular environment are incorporated into a [2Fe]<sub>F</sub>
-like precursor on HydF in the absence of HydG. We conclude that the product of HydE, presumably the dithiomethylamine ligand of [2Fe]<sub>H</sub>
, is absolutely essential to the activation process, while the diatomic products of HydG can be provided from alternate sources.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Byer</LastName>
<ForeName>Amanda S</ForeName>
<Initials>AS</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, 59717, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shepard</LastName>
<ForeName>Eric M</ForeName>
<Initials>EM</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, 59717, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ratzloff</LastName>
<ForeName>Michael W</ForeName>
<Initials>MW</Initials>
<AffiliationInfo><Affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Betz</LastName>
<ForeName>Jeremiah N</ForeName>
<Initials>JN</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, 59717, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>King</LastName>
<ForeName>Paul W</ForeName>
<Initials>PW</Initials>
<AffiliationInfo><Affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Broderick</LastName>
<ForeName>William E</ForeName>
<Initials>WE</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, 59717, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Broderick</LastName>
<ForeName>Joan B</ForeName>
<Initials>JB</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, 59717, USA. jbroderick@chemistry.montana.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
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<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>09</Month>
<Day>06</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Germany</Country>
<MedlineTA>J Biol Inorg Chem</MedlineTA>
<NlmUniqueID>9616326</NlmUniqueID>
<ISSNLinking>0949-8257</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>7LP2MPO46S</RegistryNumber>
<NameOfSubstance UI="D012436">S-Adenosylmethionine</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D046969" MajorTopicYN="N">Clostridium acetobutylicum</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006864" MajorTopicYN="N">Hydrogenase</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
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H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.

H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.

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