Archives of Microbiology

, Volume 126, Issue 2, pp 155–159 | Cite as

Effects of molybdenum and tungsten on induction of nitrate reductase and formate dehydrogenase in wild type and mutant Paracoccus denitrificans

  • Kathleen A. Burke
  • Kathleen Calder
  • June Lascelles


Molybdenum is required for induction of nitrate reductase and of NAD-linked formate dehydrogenase activities in suspensions of wild type Paracoccus denitrificans; tungsten prevents the development of these enzyme activities. The wild type forms a membrane protein Mr150,000 when incubated with tungsten and inducers of nitrate reductase and this is presumed to represent an inactive form of the enzyme. Suspensions of mutant M-1 did not develop nitrate reductase or formate dehydrogenase activities but the membrane protein Mr150,000 was formed under all conditions tested, including without inducers and without molybdenum. Analysis of membranes, solubilized with deoxycholate, by polyacrylamide gel electrophoresis under nondenaturing conditions showed that the mutant protein had similar electrophoretic mobility to the active nitrate reductase formed by the wilde type. Autoradiography of preparations from cells incubated with 55Fe showed that the mutant and wild type proteins contained iron. However, in similar experiments with 99Mo, incorporation of molybdenum into the mutant protein was not detectable.

We conclude that mutant M-1 is defective in one or more steps required to process molybdenum for incorporation into molybdoenzymes. This failure affects the normal regulation of nitrate reductase protein with respect to the role of inducers.

Key words

Nitrate reductase Formate dehydrogenase Molybdenum Tungsten Paracoccus dentrificans Inducers Membrane proteins 

Non-Standard Abbreviations




polyacrylamide gel electrophoresis


sodium dodecyl sulfate


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Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • Kathleen A. Burke
    • 1
  • Kathleen Calder
    • 1
  • June Lascelles
    • 1
  1. 1.Department of MicrobiologyUniversity of CaliforniaLos AngelesUSA

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