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Biochemistry Research International
Volume 2010 (2010), Article ID 489892, 4 pages
Research Article

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

Department of Chemistry, University of Waterloo, Waterloo, ON, Canada N2L 3G1

Received 19 July 2009; Accepted 2 September 2009

Academic Editor: Francesca CutruzzolĂ 

Copyright © 2010 Heather J. Montgomery et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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 N G -hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation of N G -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.