Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 46, Pages 17119-17124Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0602647103
Keywords
biosynthesis; nitrogenase
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Funding
- NCRR NIH HHS [RR-01209, P41 RR001209] Funding Source: Medline
- NIGMS NIH HHS [GM-67626, R01 GM067626] Funding Source: Medline
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FeMo cofactor (FeMoco) biosynthesis is one of the most complicated processes in metalloprotein biochemistry. Here we show that Mo and homocitrate are incorporated into the Fe/S core of the FeMoco precursor while it is bound to NifEN and that the resulting fully complemented, FeMoco-like cluster is transformed into a mature FeMoco upon transfer from NifEN to MoFe protein through direct protein-protein interaction. Our findings riot only clarify the process of FeMoco maturation, but also provide useful insights into the other facets of nitrogenase chemistry.
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