Divergent Members of the Nitrogenase Superfamily: Tetrapyrrole Biosynthesis and Beyond

Ghebreamlak, Selamawit M.; Mansoorabadi, Steven O.

doi:10.1002/cbic.201900782

Title: Divergent Members of the Nitrogenase Superfamily: Tetrapyrrole Biosynthesis and Beyond

Journal Article · 15 March 2020 · ChemBioChem: a European journal of chemical biology

DOI: https://doi.org/10.1002/cbic.201900782 · OSTI ID:1656752

Ghebreamlak, Selamawit M. ^[1];

^[2]

Auburn University, AL (United States); Auburn University
Auburn University, AL (United States)

The nitrogenase superfamily constitutes a large and diverse ensemble of two–component metalloenzymes. These systems couple the hydrolysis of ATP to the reduction of disparate substrates from diatomic gases (Mo and alternative nitrogenases) to photosynthetic pigments (protochlorophyllide and chlorophyllide oxidoreductases). Only very recently have the activities of the highly divergent and paraphyletic Group IV nitrogenases begun to be uncovered. In conclusion, this review highlights the first characterized member of this group, which was found to catalyze an unprecedented reaction in the coenzyme F430 biosynthetic pathway, and the catalytic potential of a superfamily that has yet to be fully explored.

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Research Organization:: Auburn University, AL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC0018043

OSTI ID:: 1656752

Alternate ID(s):: OSTI ID: 1633690

Journal Information:: ChemBioChem: a European journal of chemical biology, Journal Name: ChemBioChem: a European journal of chemical biology Journal Issue: 12 Vol. 21; ISSN 1439-4227

Publisher:: ChemPubSoc EuropeCopyright Statement

Country of Publication:: United States

Language:: English

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