| Literature DB >> 1400166 |
I Böhm1, A Halbherr, S Smaglinski, A Ernst, P Böger.
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.Entities:
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Year: 1992 PMID: 1400166 PMCID: PMC207685 DOI: 10.1128/jb.174.19.6179-6183.1992
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490