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ADP ‐ribosylation, a mechanism regulating nitrogenase activity
Author(s) -
Nordlund Stefan,
Högbom Martin
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12279
Subject(s) - nitrogenase , adp ribosylation , transferase , nitrogen fixation , enzyme , chemistry , biochemistry , reductase , microbiology and biotechnology , nitrogen , biology , nad+ kinase , organic chemistry
Nitrogen fixation is the vital biochemical process in which atmospheric molecular nitrogen is made available to the biosphere. The process is highly energetically costly and thus tightly regulated. The activity of the key enzyme, nitrogenase, is controlled by reversible mono‐ ADP ‐ribosylation of one of its components, the F e protein. This protein provides the other component, the M o F e protein, with the electrons required for the reduction of molecular nitrogen. The F e‐protein is ADP ‐ribosylated and de‐ ADP ‐ribosylated by dinitrogenase reductase ADP ‐ribosyl transferase and dinitrogenase reductase activating glycohydrolase, respectively. Here we review the current biochemical and structural knowledge of this central regulatory reaction.