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ADP-ribosylation, a mechanism regulating nitrogenase activity
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2013 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 280, no 15, 3484-3490 p.Article, review/survey (Refereed) Published
Abstract [en]

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 Fe protein. This protein provides the other component, the MoFe protein, with the electrons required for the reduction of molecular nitrogen. The Fe-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.

Place, publisher, year, edition, pages
2013. Vol. 280, no 15, 3484-3490 p.
Keyword [en]
activity regulation, crystallography, DraG, DraT, manganese, metalloprotein, nitrogenase, nitrogen fixation, post-translational modification, Rhodospirillum rubrum
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-97672DOI: 10.1111/febs.12279ISI: 000327129100002OAI: diva2:680116


Available from: 2013-12-17 Created: 2013-12-16 Last updated: 2013-12-17Bibliographically approved

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Nordlund, StefanHögbom, Martin
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