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Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion.
Συγγραφείς: Ribbe MW; Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697, USA., Bursey EH, Burgess BK
Πηγή: The Journal of biological chemistry [J Biol Chem] 2000 Jun 09; Vol. 275 (23), pp. 17631-8.
Τύπος έκδοσης: Journal Article; Research Support, U.S. Gov't, P.H.S.
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Imprint Name(s): Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
Ιατρικοί όροι (MeSH): Glutamic Acid*, Azotobacter vinelandii/*enzymology , Molybdoferredoxin/*chemistry , Molybdoferredoxin/*metabolism , Nitrogenase/*chemistry , Nitrogenase/*metabolism, Adenosine Diphosphate/metabolism ; Azotobacter vinelandii/growth & development ; Iron/metabolism ; Oxidoreductases/chemistry ; Oxidoreductases/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Computer Simulation ; Electron Spin Resonance Spectroscopy ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Sequence Alignment ; Sequence Homology, Amino Acid
Περίληψη: The Fe protein of nitrogenase has three separate functions. Much is known about the regions of the protein that are critical to its function as an electron donor to the MoFe protein, but almost nothing is known about the regions of the protein that are critical to its functions in either FeMo cofactor biosynthesis or FeMo cofactor insertion. Using computer modeling and information obtained from Fe protein mutants that were made decades ago by chemical mutagenesis, we targeted a surface residue Glu(146) as potentially being involved in FeMo cofactor biosynthesis and/or insertion. The Azotobacter vinelandii strain expressing an E146D Fe protein variant grows at approximately 50% of the wild type rate. The purified E146D Fe protein is fully functional as an electron donor to the MoFe protein, but the MoFe protein synthesized by that strain is partially ( approximately 50%) FeMo cofactor-deficient. The E146D Fe protein is fully functional in an in vitro FeMo cofactor biosynthesis assay, and the strain expressing this protein accumulates "free" FeMo cofactor. Assays that compared the ability of wild type and E146D Fe proteins to participate in FeMo cofactor insertion demonstrate, however, that the mutant is severely altered in this last reaction. This is the first known mutation that only influences the insertion reaction.
Grant Information: GM-43144 United States GM NIGMS NIH HHS
Substance Nomenclature: 0 (Molybdoferredoxin)
3KX376GY7L (Glutamic Acid)
61D2G4IYVH (Adenosine Diphosphate)
E1UOL152H7 (Iron)
EC 1.- (Oxidoreductases)
EC 1.18.6.1 (Nitrogenase)
EC 1.18.6.1 (nitrogenase reductase)
Entry Date(s): Date Created: 20000606 Date Completed: 20000720 Latest Revision: 20210209
Update Code: 20260130
DOI: 10.1074/jbc.275.23.17631
PMID: 10837496
Βάση Δεδομένων: MEDLINE
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  – Url: https://www.doi.org/10.1074/jbc.275.23.17631?
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Items – Name: Title
  Label: Title
  Group: Ti
  Data: Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AU" term="%22Ribbe+MW%22">Ribbe MW</searchLink>; Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697, USA.<br /><searchLink fieldCode="AU" term="%22Bursey+EH%22">Bursey EH</searchLink><br /><searchLink fieldCode="AU" term="%22Burgess+BK%22">Burgess BK</searchLink>
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  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2000 Jun 09; Vol. 275 (23), pp. 17631-8.
– Name: TypePub
  Label: Publication Type
  Group: TypPub
  Data: Journal Article; Research Support, U.S. Gov't, P.H.S.
– Name: Language
  Label: Language
  Group: Lang
  Data: English
– Name: TitleSource
  Label: Journal Info
  Group: Src
  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier+Inc%2E+on+behalf+of+American+Society+for+Biochemistry+and+Molecular+Biology%22">Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>2985121R <i>Publication Model: </i>Print <i>Cited Medium: </i>Print <i>ISSN: </i>0021-9258 (Print) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200219258%22">00219258 </searchLink><i>NLM ISO Abbreviation: </i>J Biol Chem <i>Subsets: </i>MEDLINE
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  Label: Imprint Name(s)
  Group: PubInfo
  Data: <i>Publication</i>: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology<br /><i>Original Publication</i>: Baltimore, MD : American Society for Biochemistry and Molecular Biology
– Name: SubjectMESH
  Label: MeSH Terms
  Group: Su
  Data: <searchLink fieldCode="MM" term="%22Glutamic+Acid%22">Glutamic Acid*</searchLink><br /><searchLink fieldCode="MM" term="%22Azotobacter+vinelandii%22">Azotobacter vinelandii</searchLink>/<searchLink fieldCode="MM" term="%22Azotobacter+vinelandii+enzymology%22">*enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Molybdoferredoxin%22">Molybdoferredoxin</searchLink>/<searchLink fieldCode="MM" term="%22Molybdoferredoxin+chemistry%22">*chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Molybdoferredoxin%22">Molybdoferredoxin</searchLink>/<searchLink fieldCode="MM" term="%22Molybdoferredoxin+metabolism%22">*metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Nitrogenase%22">Nitrogenase</searchLink>/<searchLink fieldCode="MM" term="%22Nitrogenase+chemistry%22">*chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Nitrogenase%22">Nitrogenase</searchLink>/<searchLink fieldCode="MM" term="%22Nitrogenase+metabolism%22">*metabolism</searchLink><br /><searchLink fieldCode="MH" term="%22Adenosine+Diphosphate%22">Adenosine Diphosphate</searchLink>/<searchLink fieldCode="MH" term="%22Adenosine+Diphosphate+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Azotobacter+vinelandii%22">Azotobacter vinelandii</searchLink>/<searchLink fieldCode="MH" term="%22Azotobacter+vinelandii+growth+%26+development%22">growth & development</searchLink> ; <searchLink fieldCode="MH" term="%22Iron%22">Iron</searchLink>/<searchLink fieldCode="MH" term="%22Iron+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Oxidoreductases%22">Oxidoreductases</searchLink>/<searchLink fieldCode="MH" term="%22Oxidoreductases+chemistry%22">chemistry</searchLink> ; <searchLink fieldCode="MH" term="%22Oxidoreductases%22">Oxidoreductases</searchLink>/<searchLink fieldCode="MH" term="%22Oxidoreductases+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Amino+Acid+Sequence%22">Amino Acid Sequence</searchLink> ; <searchLink fieldCode="MH" term="%22Amino+Acid+Substitution%22">Amino Acid Substitution</searchLink> ; <searchLink fieldCode="MH" term="%22Computer+Simulation%22">Computer Simulation</searchLink> ; <searchLink fieldCode="MH" term="%22Electron+Spin+Resonance+Spectroscopy%22">Electron Spin Resonance Spectroscopy</searchLink> ; <searchLink fieldCode="MH" term="%22Kinetics%22">Kinetics</searchLink> ; <searchLink fieldCode="MH" term="%22Models%2C+Molecular%22">Models, Molecular</searchLink> ; <searchLink fieldCode="MH" term="%22Molecular+Sequence+Data%22">Molecular Sequence Data</searchLink> ; <searchLink fieldCode="MH" term="%22Mutagenesis%2C+Site-Directed%22">Mutagenesis, Site-Directed</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Conformation%22">Protein Conformation</searchLink> ; <searchLink fieldCode="MH" term="%22Sequence+Alignment%22">Sequence Alignment</searchLink> ; <searchLink fieldCode="MH" term="%22Sequence+Homology%2C+Amino+Acid%22">Sequence Homology, Amino Acid</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The Fe protein of nitrogenase has three separate functions. Much is known about the regions of the protein that are critical to its function as an electron donor to the MoFe protein, but almost nothing is known about the regions of the protein that are critical to its functions in either FeMo cofactor biosynthesis or FeMo cofactor insertion. Using computer modeling and information obtained from Fe protein mutants that were made decades ago by chemical mutagenesis, we targeted a surface residue Glu(146) as potentially being involved in FeMo cofactor biosynthesis and/or insertion. The Azotobacter vinelandii strain expressing an E146D Fe protein variant grows at approximately 50% of the wild type rate. The purified E146D Fe protein is fully functional as an electron donor to the MoFe protein, but the MoFe protein synthesized by that strain is partially ( approximately 50%) FeMo cofactor-deficient. The E146D Fe protein is fully functional in an in vitro FeMo cofactor biosynthesis assay, and the strain expressing this protein accumulates "free" FeMo cofactor. Assays that compared the ability of wild type and E146D Fe proteins to participate in FeMo cofactor insertion demonstrate, however, that the mutant is severely altered in this last reaction. This is the first known mutation that only influences the insertion reaction.
– Name: GrantInfo
  Label: Grant Information
  Group: Grant
  Data: GM-43144 United States GM NIGMS NIH HHS
– Name: NumberCAS
  Label: Substance Nomenclature
  Group: ID
  Data: 0 (Molybdoferredoxin)<br />3KX376GY7L (Glutamic Acid)<br />61D2G4IYVH (Adenosine Diphosphate)<br />E1UOL152H7 (Iron)<br />EC 1.- (Oxidoreductases)<br />EC 1.18.6.1 (Nitrogenase)<br />EC 1.18.6.1 (nitrogenase reductase)
– Name: DateEntry
  Label: Entry Date(s)
  Group: Date
  Data: <i>Date Created: </i>20000606 <i>Date Completed: </i>20000720 <i>Latest Revision: </i>20210209
– Name: DateUpdate
  Label: Update Code
  Group: Date
  Data: 20260130
– Name: DOI
  Label: DOI
  Group: ID
  Data: 10.1074/jbc.275.23.17631
– Name: AN
  Label: PMID
  Group: ID
  Data: 10837496
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=cmedm&AN=10837496
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1074/jbc.275.23.17631
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 17631
    Subjects:
      – SubjectFull: Adenosine Diphosphate metabolism
        Type: general
      – SubjectFull: Azotobacter vinelandii growth & development
        Type: general
      – SubjectFull: Iron metabolism
        Type: general
      – SubjectFull: Oxidoreductases chemistry
        Type: general
      – SubjectFull: Oxidoreductases metabolism
        Type: general
      – SubjectFull: Amino Acid Sequence
        Type: general
      – SubjectFull: Amino Acid Substitution
        Type: general
      – SubjectFull: Computer Simulation
        Type: general
      – SubjectFull: Electron Spin Resonance Spectroscopy
        Type: general
      – SubjectFull: Kinetics
        Type: general
      – SubjectFull: Models, Molecular
        Type: general
      – SubjectFull: Molecular Sequence Data
        Type: general
      – SubjectFull: Mutagenesis, Site-Directed
        Type: general
      – SubjectFull: Protein Conformation
        Type: general
      – SubjectFull: Sequence Alignment
        Type: general
      – SubjectFull: Sequence Homology, Amino Acid
        Type: general
      – SubjectFull: Glutamic Acid
        Type: general
      – SubjectFull: Azotobacter vinelandii enzymology
        Type: general
      – SubjectFull: Molybdoferredoxin chemistry
        Type: general
      – SubjectFull: Molybdoferredoxin metabolism
        Type: general
      – SubjectFull: Nitrogenase chemistry
        Type: general
      – SubjectFull: Nitrogenase metabolism
        Type: general
    Titles:
      – TitleFull: Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Ribbe MW
      – PersonEntity:
          Name:
            NameFull: Bursey EH
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            NameFull: Burgess BK
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          Dates:
            – D: 09
              M: 06
              Text: 2000 Jun 09
              Type: published
              Y: 2000
          Identifiers:
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              Value: 0021-9258
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              Value: 275
            – Type: issue
              Value: 23
          Titles:
            – TitleFull: The Journal of biological chemistry
              Type: main
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