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Nitrogenase Fe protein: A molybdate/homocitrate insertase.

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 26, 2006

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The Fe protein mobilizes molybdenum/homocitrate for iron-molybdenum cofactor (FeMoco) maturation. This process, crucial for nitrogenase, involves MgATP hydrolysis and interaction with NifEN.

Area of Science:

Biochemistry
Nitrogen Fixation
Metalloprotein Assembly

Background:

The Fe protein is essential for nitrogenase function.
The precise role of the Fe protein in iron-molybdenum cofactor (FeMoco) biosynthesis remains unclear.

Purpose of the Study:

To elucidate the function of the Fe protein in FeMoco biosynthesis.
To understand the mechanism of metal trafficking in metalloprotein assembly.

Main Methods:

Investigated the interaction between Fe protein, NifEN, and Mo/homocitrate.
Analyzed the role of MgATP hydrolysis in the process.

Main Results:

The Fe protein acts as a Mo/homocitrate insertase, mobilizing the cofactor for FeMoco precursor maturation on NifEN.

Related Experiment Videos

Mo/homocitrate mobilization is dependent on MgATP hydrolysis and Fe protein-NifEN interaction.

Conclusions:

The Fe protein has a dual role in nitrogenase activity and FeMoco assembly.
This study reveals a novel mechanism for metal trafficking in the biosynthesis of complex metalloproteins.