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Investigations of succinate dehydrogenase and fumarate reductase in whole cells ofShewanella putrefaciens (strains MR-1 and MR-7) using electron spin resonance spectroscopy

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Abstract

Using ESR spectroscopy we were able to detect succinate dehydrogenase (SDH) in the whole cells ofShewanella putrefaciens grown aerobically. ESR analysis of cells grown under anaerobic conditions in the presence of fumarate as electron acceptor revealed signals with the same parameters as SDH. However the temperature dependence was quite different. Furthermore, the addition of sodium azide led to disappearance of this ESR signal in anaerobic cultures, while the same treatment of aerobic cultures had no effect on the ESR signal of SDH. Based on these results, we postulate that the ESR signal from the anaerobic cells is that of fumarate reductase, similar in its properties to the fumarate reductase fromEscherichia coli.

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Authors and Affiliations

  1. Institute of Chemical Physics, Moscow, Russian Federation

    D. S. Burbaev

  2. Department of Biology, Moscow State University, Moscow, Russian Federation

    O. I. Keppen

  3. University Wisconsin-Milwaukee Center for Great Lakes Studies, 600 E. Greenfield av., 53204, Milwaukee, WI, USA

    A. I. Tsapin & K. H. Nealson

Authors
  1. A. I. Tsapin
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  2. D. S. Burbaev
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  3. K. H. Nealson
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  4. O. I. Keppen
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Tsapin, A.I., Burbaev, D.S., Nealson, K.H. et al. Investigations of succinate dehydrogenase and fumarate reductase in whole cells ofShewanella putrefaciens (strains MR-1 and MR-7) using electron spin resonance spectroscopy. Appl. Magn. Reson. 9, 509–516 (1995). https://doi.org/10.1007/BF03162358

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  • DOI: https://doi.org/10.1007/BF03162358

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