Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

FeMo cofactor maturation on NifEN.

Yilin Hu1, Mary C Corbett, Aaron W Fay

  • 1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 20, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Impact of N-terminal acetylation on Cu(I) coordination by alpha synuclein protein.

Journal of inorganic biochemistry·2026
Same author

Mechanism of O<sub>2</sub> Activation and Cysteine Oxidation by the Unusual Mononuclear Cu(I) Active Site of the Formylglycine-Generating Enzyme.

ACS central science·2025
Same author

Experimental electronic structures of the Fe<sup>IV</sup>=O bond in S=1 heme vs. nonheme sites: Effect of the porphyrin ligand.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Synthesis, Structure, and Redox Reactivity of Ni Complexes Bearing a Redox and Acid-Base Non-innocent Ligand with Ni<sup>II</sup>, Ni<sup>III</sup>, and Ni<sup>IV</sup> Formal Oxidation States.

Journal of the American Chemical Society·2025
Same author

Experimental Definition of the <i>S</i> = 1 π vs <i>S</i> = 2 σ Reactivity and <i>S</i> = 2 Character in the Ground State of an <i>S</i> = 1 Fe<sup>IV</sup>O Complex.

Journal of the American Chemical Society·2024
Same author

Heterologous synthesis of the complex homometallic cores of nitrogenase P- and M-clusters in <i>Escherichia coli</i>.

Proceedings of the National Academy of Sciences of the United States of America·2023
Same journal

In This Issue.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Long-term cultural continuity across the Neanderthal-modern human sequence at Üçağızlı II Cave, northern Levant.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Dolphins use names to remember whom to avoid.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Retraction for Shaked and Frenkel, Curiouser and curiouser: Meningeal lymphoid structures in the aging brain.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Small but mighty: The outsized role of small water bodies in the global carbon cycle.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Functional traits produce conditional outcomes in different community contexts.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

The biosynthesis of the iron-molybdenum cofactor (FeMoco) involves its maturation within the NifEN complex. The FeMoco precursor is then transferred to the MoFe protein for final maturation, clarifying nitrogenase chemistry.

Area of Science:

  • Biochemistry
  • Metalloprotein Chemistry
  • Nitrogenase Research

Background:

  • FeMo cofactor (FeMoco) biosynthesis is a complex metalloprotein process.
  • Understanding FeMoco maturation is crucial for nitrogenase function.

Purpose of the Study:

  • To elucidate the mechanism of FeMoco maturation.
  • To clarify the roles of NifEN and MoFe proteins in FeMoco assembly.

Main Methods:

  • Investigated the incorporation of molybdenum and homocitrate into the Fe/S core of the FeMoco precursor.
  • Studied the transfer of the FeMoco-like cluster from NifEN to the MoFe protein.

Main Results:

  • Molybdenum and homocitrate are incorporated into the Fe/S core of the FeMoco precursor while bound to NifEN.

Related Experiment Videos

  • A fully complemented, FeMoco-like cluster is formed within NifEN.
  • The cluster matures into FeMoco upon transfer to the MoFe protein via direct protein-protein interaction.

    • Conclusions:

    • The NifEN complex plays a key role in the initial stages of FeMoco maturation.
    • Direct protein-protein interaction facilitates the transfer and final maturation of FeMoco.
    • Findings provide insights into nitrogenase chemistry and metalloprotein biochemistry.