TITLE

Cloning, Expression, and Purification of a Nitric Oxide Synthase-Like Protein from Bacillus cereus

AUTHOR(S)
Montgomery, Heather J.; Dupont, Andrea L.; Leivo, Hilary E.; Guillemette, J. Guy
PUB. DATE
January 2010
SOURCE
Biochemistry Research International;2010, p1
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The nitric oxide synthase-like protein from Bacillus cereus (bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer. The recombinant protein showed similar spectral shifts to the mammalian NOS proteins and could bind the substrates L-arginine and NG-hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation of NG-hydroxy-L-arginine and L-arginine by bcNOS, while a reconstituted system with the rat neuronal NOS reductase domain showed no activity. The recombinant bcNOS protein adds to the complement of bacterial NOS-like proteins that are used for the investigation of the mechanism and function of NO in microorganisms.
ACCESSION #
56530496

 

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