The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions.
Identifieur interne : 000016 ( Main/Exploration ); précédent : 000015; suivant : 000017The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions.
Auteurs : Brigitta Németh [Suède] ; Henrik Land [Suède] ; Ann Magnuson [Suède] ; Anders Hofer [Suède] ; Gustav Berggren [Suède]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2020.
Abstract
[FeFe] hydrogenases have attracted extensive attention in the field of renewable energy research because of their remarkable efficiency for H2 gas production. H2 formation is catalyzed by a biologically unique hexanuclear iron cofactor denoted the H-cluster. The assembly of this cofactor requires a dedicated maturation machinery including HydF, a multidomain [4Fe4S] cluster protein with GTPase activity. HydF is responsible for harboring and delivering a precatalyst to the apo-hydrogenase, but the details of this process are not well understood. Here, we utilize gas-phase electrophoretic macromolecule analysis to show that a HydF dimer forms a transient interaction complex with the hydrogenase and that the formation of this complex depends on the cofactor content on HydF. Moreover, Fourier transform infrared, electron paramagnetic resonance, and UV-visible spectroscopy studies of mutants of HydF show that the isolated iron-sulfur cluster domain retains the capacity for binding the precatalyst in a reversible fashion and is capable of activating apo-hydrogenase in in vitro assays. These results demonstrate the central role of the iron-sulfur cluster domain of HydF in the final stages of H-cluster assembly, i.e. in binding and delivering the precatalyst.
DOI: 10.1074/jbc.RA119.011419
PubMed: 32620553
PubMed Central: PMC7450098
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Land</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala</wicri:regionArea><orgName type="university">Université d'Uppsala</orgName><placeName><settlement type="city">Uppsala</settlement><region nuts="1">Svealand</region><region nuts="1">East Middle Sweden</region></placeName></affiliation></author><author><name sortKey="Magnuson, Ann" sort="Magnuson, Ann" uniqKey="Magnuson A" first="Ann" last="Magnuson">Ann Magnuson</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala</wicri:regionArea><orgName type="university">Université 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wicri:rule="url">Suède</country><wicri:regionArea>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala</wicri:regionArea><orgName type="university">Université d'Uppsala</orgName><placeName><settlement type="city">Uppsala</settlement><region nuts="1">Svealand</region><region nuts="1">East Middle Sweden</region></placeName></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">[FeFe] hydrogenases have attracted extensive attention in the field of renewable energy research because of their remarkable efficiency for H<sub>2</sub> gas production. H<sub>2</sub> formation is catalyzed by a biologically unique hexanuclear iron cofactor denoted the H-cluster. The assembly of this cofactor requires a dedicated maturation machinery including HydF, a multidomain [4Fe4S] cluster protein with GTPase activity. HydF is responsible for harboring and delivering a precatalyst to the apo-hydrogenase, but the details of this process are not well understood. Here, we utilize gas-phase electrophoretic macromolecule analysis to show that a HydF dimer forms a transient interaction complex with the hydrogenase and that the formation of this complex depends on the cofactor content on HydF. Moreover, Fourier transform infrared, electron paramagnetic resonance, and UV-visible spectroscopy studies of mutants of HydF show that the isolated iron-sulfur cluster domain retains the capacity for binding the precatalyst in a reversible fashion and is capable of activating apo-hydrogenase in <i>in vitro</i> assays. These results demonstrate the central role of the iron-sulfur cluster domain of HydF in the final stages of H-cluster assembly, <i>i.e.</i> in binding and delivering the precatalyst.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32620553</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>295</Volume><Issue>33</Issue><PubDate><Year>2020</Year><Month>Aug</Month><Day>14</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions.</ArticleTitle><Pagination><MedlinePgn>11891-11901</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA119.011419</ELocationID><Abstract><AbstractText>[FeFe] hydrogenases have attracted extensive attention in the field of renewable energy research because of their remarkable efficiency for H<sub>2</sub> gas production. H<sub>2</sub> formation is catalyzed by a biologically unique hexanuclear iron cofactor denoted the H-cluster. The assembly of this cofactor requires a dedicated maturation machinery including HydF, a multidomain [4Fe4S] cluster protein with GTPase activity. HydF is responsible for harboring and delivering a precatalyst to the apo-hydrogenase, but the details of this process are not well understood. Here, we utilize gas-phase electrophoretic macromolecule analysis to show that a HydF dimer forms a transient interaction complex with the hydrogenase and that the formation of this complex depends on the cofactor content on HydF. Moreover, Fourier transform infrared, electron paramagnetic resonance, and UV-visible spectroscopy studies of mutants of HydF show that the isolated iron-sulfur cluster domain retains the capacity for binding the precatalyst in a reversible fashion and is capable of activating apo-hydrogenase in <i>in vitro</i> assays. These results demonstrate the central role of the iron-sulfur cluster domain of HydF in the final stages of H-cluster assembly, <i>i.e.</i> in binding and delivering the precatalyst.</AbstractText><CopyrightInformation>© 2020 Németh et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Németh</LastName><ForeName>Brigitta</ForeName><Initials>B</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-7586-6736</Identifier><AffiliationInfo><Affiliation>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Land</LastName><ForeName>Henrik</ForeName><Initials>H</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-3073-5641</Identifier><AffiliationInfo><Affiliation>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Magnuson</LastName><ForeName>Ann</ForeName><Initials>A</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-7918-4441</Identifier><AffiliationInfo><Affiliation>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hofer</LastName><ForeName>Anders</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berggren</LastName><ForeName>Gustav</ForeName><Initials>G</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-6717-6612</Identifier><AffiliationInfo><Affiliation>Department of Chemistry-Ångström Laboratory, Uppsala University, Uppsala, Sweden Gustav.berggren@kemi.uu.se.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList 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