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Hydrogen metabolism in isolated heterocysts of Anabaena 7120

Hydrogen metabolism in isolated heterocysts of Anabaena 7120 203 116 116 2 2 R. B. Peterson R. H. Burris Department of Biochemistry, College of Agricultural and Life Sciences University of Wisconsin-Madison 420 Henry Mall 53706 Madison WI U.S.A. Abstract Isolated heterocysts of Anabaena 7120 evolve H 2 in an ATP-dependent nitrogenase-catalyzed process that is inhibited by N 2 and C 2 H 2 . Heterocysts have an active uptake hydrogenase that only requires an electron acceptor of positive redox potential, e.g., methylene blue, dichlorophenolindophenol or potassium ferricyanide. O 2 supplied at low partial pressures is a very effective physiological oxidant for H 2 uptake. High concentrations of O 2 are inhibitory to H 2 uptake. The oxyhydrogen reaction in heterocysts appears to be mediated by a cytochrome-cytochrome oxidase system, and it supports ATP synthesis via oxidative phosphorylation. Attempts to demonstrate acetylene reduction in isolated heterocysts employing H 2 as an electron donor were unsuccessful. It is suggested that the uptake hydrogenase functions to conserve reductant that otherwise would be dissipated via nitrogenase-catalyzed H 2 evolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

Hydrogen metabolism in isolated heterocysts of Anabaena 7120

Peterson, R.; Burris, R.
Archives of Microbiology , Volume 116 (2) – Feb 1, 1978
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References (39)

Publisher
Springer Journals
Copyright
Copyright © 1978 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00406027
Publisher site
See Article on Publisher Site

Abstract

203 116 116 2 2 R. B. Peterson R. H. Burris Department of Biochemistry, College of Agricultural and Life Sciences University of Wisconsin-Madison 420 Henry Mall 53706 Madison WI U.S.A. Abstract Isolated heterocysts of Anabaena 7120 evolve H 2 in an ATP-dependent nitrogenase-catalyzed process that is inhibited by N 2 and C 2 H 2 . Heterocysts have an active uptake hydrogenase that only requires an electron acceptor of positive redox potential, e.g., methylene blue, dichlorophenolindophenol or potassium ferricyanide. O 2 supplied at low partial pressures is a very effective physiological oxidant for H 2 uptake. High concentrations of O 2 are inhibitory to H 2 uptake. The oxyhydrogen reaction in heterocysts appears to be mediated by a cytochrome-cytochrome oxidase system, and it supports ATP synthesis via oxidative phosphorylation. Attempts to demonstrate acetylene reduction in isolated heterocysts employing H 2 as an electron donor were unsuccessful. It is suggested that the uptake hydrogenase functions to conserve reductant that otherwise would be dissipated via nitrogenase-catalyzed H 2 evolution.

Journal

Archives of Microbiology – Springer Journals

Published: Feb 1, 1978

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