Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 9, Pages 3236-3241Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0409201102
Keywords
Fe protein; FeMoco; MoFe protein
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Funding
- NIGMS NIH HHS [GM-67626, R01 GM067626] Funding Source: Medline
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The biosynthesis of the FeMo cofactor (FeMoco) of Azotobacter vinelandii nitrogenase presumably starts with the production of its Fe/S core by NifB (the nifB gene product). This core is subsequently processed on the alpha(2)beta(2) tetrameric NifEN complex (formed by the nifE and nifty gene products). In this article, we identify a NifEN-bound FeMoco precursor form that can be converted to fully assembled FeMoco in a so-called FeMoco-maturation assay containing only purified components. We also establish that only molybdate, homocitrate, MgATP, and Fe protein are essential for FeMoco maturation. The FeMoco-maturation assay described here will further address the remaining questions related to the assembly mechanism of the ever-intriguing FeMoco.
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