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Journal of Bacteriology, November 2002, p. 5898-5902, Vol. 184, No. 21
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.21.5898-5902.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Hydroxylamine Reductase Activity of the Hybrid Cluster Protein from Escherichia coli

Marcus T. Wolfe,1 Jongyun Heo,2 John S. Garavelli,3 and Paul W. Ludden1*

Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, Madison, Wisconsin 53706,1 Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599,2 RESID Database, Washington, D.C. 200073

Received 28 February 2002/ Accepted 10 July 2002

The hybrid cluster protein (HCP; formerly termed the prismane protein) has been extensively studied due to its unique spectroscopic properties. Although the structural and spectroscopic characteristics are well defined, its enzymatic function, up to this point, has remained unidentified. While it was proposed that HCP acts in some step of nitrogen metabolism, a specific role for this enzyme remained unknown. Recent studies of HCP purified from Escherichia coli have identified a novel hydroxylamine reductase activity. These data reveal the ability of HCP to reduce hydroxylamine in vitro to form NH3 and H2O. Further biochemical analyses were completed in order to determine the effects of various electron donors, different pH levels, and the presence of CN- on in vitro hydroxylamine reduction.

* Corresponding author. Present address: College of Natural Resources, 101 Giannini Hall #3100, UC Berkeley, Berkeley, CA 94720-3100. Phone: (510) 642-7171. Fax: (510) 642-4612. E-mail: pludden{at}nature.berkeley.edu.

Journal of Bacteriology, November 2002, p. 5898-5902, Vol. 184, No. 21
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.21.5898-5902.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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