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Divergent Members of the Nitrogenase Superfamily: Tetrapyrrole Biosynthesis and Beyond
Author(s) -
Ghebreamlak Selamawit M.,
Mansoorabadi Steven O.
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900782
Subject(s) - tetrapyrrole , nitrogenase , superfamily , cofactor , protochlorophyllide , biosynthesis , biochemistry , chemistry , haloarchaea , stereochemistry , biology , archaea , enzyme , genetics , nitrogen fixation , bacteria , gene
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. 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.