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PMID: 16592599 Published · ppublish English Journal Article

High recovery of nitrogenase activity and of Fe-labeled nitrogenase in heterocysts isolated from Anabaena variabilis.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 12 ·1978-12-00 ·Pages 6271-5

Peterson RB, Wolk CP

Abstract

Heterocysts were isolated from the N(2)-fixing cyanobacterium Anabaena variabilis after vegetative cells were disrupted by treatment with lysozyme and cavitation in a sonic cleaning bath. The acetylene-reducing (nitrogenase) activity of the isolated heterocysts, ca. 5.0 mumol (mg of chlorophyll a)(-1) min(-1) in the presence of H(2) and light, accounted for an average of 60% of the nitrogenase activity of whole filaments, and was relatively insensitive to inactivation by oxygen. Soluble extracts derived from intact filaments grown with (55)Fe, and from their heterocysts and vegetative cells, were subjected to electrophoresis. The nitrogenase and nitrogenase reductase bands (MoFe protein and Fe protein, or component 1 and component 2, respectively) were identified in these nondenaturing gels, and their radioactivities were quantitated. The isolated heterocysts accounted for an average of 91% of the nitrogenase and 69% of the nitrogenase reductase of the original filaments.

Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Peterson R B
MSU-DOE Plant Research Laboratory, East Lansing, Michigan 48824.
Wolk C P
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.75.12.6271
Published
1978-12-00
Pages
6271-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC393163
External Links
PubMed source DOI: 10.1073/pnas.75.12.6271 PMC Full Text View journal details
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