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Journal of Bacteriology, November 2002, p. 5894-5897, Vol. 184, No. 21
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.21.5894-5897.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Converting the NiFeS Carbon Monoxide Dehydrogenase to a Hydrogenase and a Hydroxylamine Reductase

Jongyun Heo,1 Marcus T. Wolfe,2 Christopher R. Staples,3 and Paul W. Ludden2*

Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260,1 Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin—Madison, Madison, Wisconsin 53706-1544,2 Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-16043

Received 11 February 2002/ Accepted 5 August 2002

Substitution of one amino acid for another at the active site of an enzyme usually diminishes or eliminates the activity of the enzyme. In some cases, however, the specificity of the enzyme is changed. In this study, we report that the changing of a metal ligand at the active site of the NiFeS-containing carbon monoxide dehydrogenase (CODH) converts the enzyme to a hydrogenase or a hydroxylamine reductase. CODH with alanine substituted for Cys531 exhibits substantial uptake hydrogenase activity, and this activity is enhanced by treatment with CO. CODH with valine substituted for His265 exhibits hydroxylamine reductase activity. Both Cys531 and His265 are ligands to the active-site cluster of CODH. Further, CODH with Fe substituted for Ni at the active site acquires hydroxylamine reductase activity.

* 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. 5894-5897, Vol. 184, No. 21
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.21.5894-5897.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Raymond, J. (2005). The Evolution of Biological Carbon and Nitrogen Cycling--a Genomic Perspective. Reviews in Mineralogy and Geochemistry 59: 211-231 [Full Text]  
  • Cabello, P., Pino, C., Olmo-Mira, M. F., Castillo, F., Roldan, M. D., Moreno-Vivian, C. (2004). Hydroxylamine Assimilation by Rhodobacter capsulatus E1F1: REQUIREMENT OF THE hcp GENE (HYBRID CLUSTER PROTEIN) LOCATED IN THE NITRATE ASSIMILATION nas GENE REGION FOR HYDROXYLAMINE REDUCTION. J. Biol. Chem. 279: 45485-45494 [Abstract] [Full Text]  
  • Wolfe, M. T., Heo, J., Garavelli, J. S., Ludden, P. W. (2002). Hydroxylamine Reductase Activity of the Hybrid Cluster Protein from Escherichia coli. J. Bacteriol. 184: 5898-5902 [Abstract] [Full Text]  


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