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Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase

Wilfried Freudenberg , Kerstin König , Jan Remmer Andreesen
DOI: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02564.x 13-17 First published online: 1 July 1988

Summary

The nicotine dehydrogenase from Arthrobacter oxidans was purified 40-fold to homogeneity with 26% recovery. SDS-polyacrylamide gel electrophoresis of the enzyme revealed three protein bands corresponding to Mr of 82 000, 30 000 and 15 000. The Mr of the native enzyme was calculated to be 12 0000 by gel chromatography. The enzyme contained about 1 FAD, 1 molybdenum, 4 iron and 2 labile sulfur.

Key words
  • Arthrobacter oxidans
  • Molybdenum
  • Molybdoenzyme
  • Nicotine dehydrogenase

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