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ADP-ribosylation, a mechanism regulating nitrogenase activity
Stefan Nordlund1, Martin Högbom
1Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. stefan@dbb.su.se
The FEBS Journal
|April 12, 2013
Summary
Nitrogen fixation, essential for life, is regulated by modifying the nitrogenase enzyme. This review covers the biochemical and structural details of this crucial regulatory process.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Nitrogen fixation is a critical process for making atmospheric nitrogen available to living organisms.
- This process is energy-intensive and requires strict regulation.
- The enzyme nitrogenase catalyzes nitrogen fixation, with its activity controlled by reversible ADP-ribosylation of the Fe protein.
Purpose of the Study:
- To review the current biochemical and structural understanding of the regulation of nitrogenase activity.
- To elucidate the mechanism of reversible mono-ADP-ribosylation of the Fe protein.
- To detail the roles of dinitrogenase reductase ADP-ribosyl transferase and dinitrogenase reductase activating glycohydrolase.
Main Methods:
- Literature review of existing biochemical studies.
- Analysis of structural data related to nitrogenase and its regulatory components.
- Synthesis of current knowledge on the enzymatic mechanisms involved.
Main Results:
- Nitrogenase activity is regulated by mono-ADP-ribosylation of the Fe protein.
- This modification is catalyzed by dinitrogenase reductase ADP-ribosyl transferase.
- The reverse reaction, de-ADP-ribosylation, is performed by dinitrogenase reductase activating glycohydrolase.
Conclusions:
- The reversible ADP-ribosylation of the Fe protein is a central regulatory mechanism for nitrogen fixation.
- Understanding this process provides insight into the control of a vital biogeochemical pathway.
- Further research into the biochemical and structural aspects can reveal more about nitrogenase regulation.
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