Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 12, Issue 8, Pages 1129-1139Publisher
SPRINGER
DOI: 10.1007/s00775-007-0279-x
Keywords
molybdenum cofactor; molybdopterin; dimethyl sulfoxide reductase; nitrate reductase; copper
Funding
- NIGMS NIH HHS [GM 66236] Funding Source: Medline
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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, 2004). 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.
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