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Journal of Bacteriology, October 2001, p. 5743-5746, Vol. 183, No. 19
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.19.5743-5746.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Effects of Specific Amino Acid Substitutions on Activities of Dinitrogenase Reductase-Activating Glycohydrolase from Rhodospirillum rubrum

Babu S. Antharavally,1 Russell R. Poyner,2 Yaoping Zhang,3 Gary P. Roberts,3 and Paul W. Ludden1,*

Departments of Biochemistry1 and Bacteriology3 and Institute for Enzyme Research,2 University of Wisconsin, Madison, Wisconsin

Received 2 January 2001/Accepted 18 June 2001

Site-directed mutagenesis of the draG gene was used to generate altered forms of dinitrogenase reductase-activating glycohydrolase (DRAG) with D123A, H142L, H158N, D243G, and E279R substitutions. The amino acid residues H142 and E279 are not required either for the coordination to the metal center or for catalysis since the variants H142L and E279R retained both catalytic and electron paramagnetic resonance spectral properties similar to those of the wild-type enzyme. Since DRAG-H158N and DRAG-D243G variants lost their ability to bind Mn(II) and to catalyze the hydrolysis of the substrate, H158 and D243 residues could be involved in the coordination of the binuclear Mn(II) center in DRAG.

* Corresponding author. Mailing address: Department of Biochemistry, 433 Babcock Dr., University of Wisconsin, Madison, WI 53706. Phone: (608) 262-6859. Fax: (608) 262-3453. E-mail: ludden{at}biochem.wisc.edu.

Journal of Bacteriology, October 2001, p. 5743-5746, Vol. 183, No. 19
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.19.5743-5746.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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