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. 1992 Oct;174(19):6179–6183. doi: 10.1128/jb.174.19.6179-6183.1992

In vitro activation of dinitrogenase reductase from the cyanobacterium Anabaena variabilis (ATCC 29413).

I Böhm 1, A Halbherr 1, S Smaglinski 1, A Ernst 1, P Böger 1
PMCID: PMC207685  PMID: 1400166

Abstract

Nitrogenase of the heterocystous cyanobacterium Anabaena variabilis was inactivated in vivo (S. Reich, H. Almon, and P. Böger, FEMS Microbiol. Lett. 34:53-56, 1986). Partially purified and modified (inactivated) dinitrogenase reductase (Fe-protein) of such cells was reactivated by isolated membrane fractions of A. variabilis or of Rhodospirillum rubrum, and acetylene reduction was measured. Reactivation requires ATP, Mg2+, and Mn2+. The activating principle is localized in the heterocyst and was found effective only when prepared from cells exhibiting active nitrogenase. It also restores the activity of modified Fe-protein from R. rubrum.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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