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Dissimilatory hexaheme c nitrite reductase of “Spirillum” strain 5175: purification and properties

Dissimilatory hexaheme c nitrite reductase of “Spirillum” strain 5175: purification and properties 203 156 156 1 1 Wolfram Schumacher Peter M. H. Kroneck Fakultät Biologie Universität Konstanz W-7750 Konstanz Federal Republic of Germany Abstract When grown with nitrate as terminal electron acceptor both the soluble (periplasm, cytoplasm) and the membrane fraction of “Spirillum” strain 5175 exhibited high nitrite reductase activity. The nitrite reductase obtained from the soluble fraction was purified 76-fold to electrophoretical homogeneity. The enzyme reduced nitrite to ammonia with a specific activity of 723 μmol NO inf2 sup- × (mg protein × min) -1 . The molecular mass was 58±1 kDa by SDS-PAGE compared to 59±2 kDa determined by size exclusion chromatography under nondenaturing conditions. The enzyme (as isolated) contained 5.97±0.15 heme c molecules/M r 58 kDa. The absorption spectrum was typical for c -type cytochrome with maxima at 280, 408, 532 and 610 nm (oxidized) and at 420, 523 and 553 nm (dithionite-reduced). The enzyme (as isolated) exhibited a complex set of high-spin and lowspin ferric heme resonances with g-values at 9.82, 3,85, 3.31, 2.95, 2.30 and 1.49 in agreement with data reported for electron paramagnetic resonance spectra of nitrite reductases from Desulfovibrio desulfuricans, Wolinella succinogenes and Escherichia coli . http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

Dissimilatory hexaheme c nitrite reductase of “Spirillum” strain 5175: purification and properties

Archives of Microbiology , Volume 156 (1) – Jul 1, 1991

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References (30)

Publisher
Springer Journals
Copyright
Copyright © 1991 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00418190
Publisher site
See Article on Publisher Site

Abstract

203 156 156 1 1 Wolfram Schumacher Peter M. H. Kroneck Fakultät Biologie Universität Konstanz W-7750 Konstanz Federal Republic of Germany Abstract When grown with nitrate as terminal electron acceptor both the soluble (periplasm, cytoplasm) and the membrane fraction of “Spirillum” strain 5175 exhibited high nitrite reductase activity. The nitrite reductase obtained from the soluble fraction was purified 76-fold to electrophoretical homogeneity. The enzyme reduced nitrite to ammonia with a specific activity of 723 μmol NO inf2 sup- × (mg protein × min) -1 . The molecular mass was 58±1 kDa by SDS-PAGE compared to 59±2 kDa determined by size exclusion chromatography under nondenaturing conditions. The enzyme (as isolated) contained 5.97±0.15 heme c molecules/M r 58 kDa. The absorption spectrum was typical for c -type cytochrome with maxima at 280, 408, 532 and 610 nm (oxidized) and at 420, 523 and 553 nm (dithionite-reduced). The enzyme (as isolated) exhibited a complex set of high-spin and lowspin ferric heme resonances with g-values at 9.82, 3,85, 3.31, 2.95, 2.30 and 1.49 in agreement with data reported for electron paramagnetic resonance spectra of nitrite reductases from Desulfovibrio desulfuricans, Wolinella succinogenes and Escherichia coli .

Journal

Archives of MicrobiologySpringer Journals

Published: Jul 1, 1991

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