FeMo cofactor maturation on NifEN.
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 not only clarify the process of FeMoco maturation, but also provide useful insights into the other facets of nitrogenase chemistry.
Hu
Yilin
Y
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Corbett
Mary C
MC
Fay
Aaron W
AW
Webber
Jerome A
JA
Hodgson
Keith O
KO
Hedman
Britt
B
Ribbe
Markus W
MW
D004578:Electron Spin Resonance Spectroscopy; D008983:Molybdoferredoxin / Q000737:chemistry* / Q000378:metabolism*; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D008983:Molybdoferredoxin; D009591:Nitrogenase