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- Title
Probing the role of copper in the biosynthesis of the molybdenum cofactor in Escherichia coli and Rhodobacter sphaeroides.
- Authors
Morrison, M. Scott; Cobine, Paul A.; Hegg, Eric L.
- Abstract
The crystal structure of Cnx1G, an enzyme involved in the biosynthesis of the molybdenum cofactor (Moco) in Arabidopsis thaliana, revealed the remarkable feature of a copper ion bound to the dithiolene unit of a molybdopterin intermediate (Kuper et al. Nature 430:803–806, ). To characterize further the role of copper in Moco biosynthesis, we examined the in vivo and/or in vitro activity of two Moco-dependent enzymes, dimethyl sulfoxide reductase (DMSOR) and nitrate reductase (NR), from cells grown under a variety of copper conditions. We found the activities of DMSOR and NR were not affected when copper was depleted from the media of either Escherichia coli or Rhodobacter sphaeroides. These data suggest that while copper may be utilized during Moco biosynthesis when it is available, copper does not appear to be strictly required for Moco biosynthesis in these two organisms.
- Subjects
BIOCHEMICAL engineering; BIOSYNTHESIS; ORGANIC synthesis; BIOTECHNOLOGY; ESCHERICHIA coli; ESCHERICHIA
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2007, Vol 12, Issue 8, p1129
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-007-0279-x