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FeMo cofactor maturation on NifEN.

ABSTRACT: 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.

SUBMITTER: Hu Y

PROVIDER: S-EPMC1859895 | biostudies-other | 2006 Nov

REPOSITORIES: biostudies-other

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FeMo cofactor maturation on NifEN.

Hu Yilin Y Corbett Mary C MC Fay Aaron W AW Webber Jerome A JA Hodgson Keith O KO Hedman Britt B Ribbe Markus W MW

Proceedings of the National Academy of Sciences of the United States of America 20061018 46

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 us ...[more]

PMID: 17050696

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