Nitrogen fixation gene (nifL) involved in oxygen regulation of nitrogenase synthesis in K. peumoniae View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1981-04

AUTHORS

Susan Hill, Christina Kennedy, Eugene Kavanagh, Richard B. Goldberg, Robert Hanau

ABSTRACT

The enzyme complex nitrogenase, which reduces N2 to NH4+, involves two redox proteins, both irreversibly damaged by O2 (ref. 1). Enzyme activity therefore requires anaerobic conditions, a source of reductant and a large amount of ATP (∼16 ATPs per N2)2,3. In both aerobic and facultative anaerobic N2-fixing bacteria, nitrogenase synthesis is regulated by O2 and NH4+, but in the aerobes there are also processes to protect the enzyme from O2 damage4,5. The mechanisms of repression by O2 and NH4+ seem to be independent in the organisms so far examined6–8. In the facultative anaerobe, Klebsiella pneumoniae, O2 was shown to repress nitrogenase synthesis in an NH4+-constitutive strain8. The fusion of the Escherichia coli lacZ gene into each transcriptional unit of the nitrogen fixation (nif) gene cluster in K. pneumoniae has facilitated studies with O2, because expression from the various nif promoters results in an O2-stable product (β-galactosidase). Notably, the nifHDK operon (the nitrogenase structural genes) was more sensitive to O2 repression than the nifLA operon (regulatory genes)9. The characterization of mutants, reported here, indicates the involvement of a nif-regulatory gene product in the mechanism of O2 control of nitrogenase synthesis. More... »

PAGES

424-426

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/290424a0

DOI

http://dx.doi.org/10.1038/290424a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1035620095

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7012640


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