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