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Volume 272, Number 28, Issue of July 11, 1997 pp. 17574-17580
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Crystal Structures of Substrate Binding Site Mutants of Manganese Peroxidase

(Received for publication, March 6, 1997, and in revised form, March 24, 1997)

Munirathinam Sundaramoorthy , Katsuyuki Kishi ^§ , Michael H. Gold ^§ and Thomas L. Poulos

From the  Department of Molecular Biology & Biochemistry and Physiology & Biophysics, University of California, Irvine, California 92697-3900 and ^§ Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland, Oregon 97291-1000

Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degrading basidiomycetous fungus, Phanerochaete chrysosporium, catalyzes the oxidation of Mn^II to Mn^III. The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin model compounds. The proposed Mn^II binding site of MnP consists of a heme propionate, three acidic ligands (Glu-35, Glu-39, and Asp-179), and two water molecules. Using crystallographic methods, this binding site was probed by altering the amount of Mn^II bound to the protein. Crystals grown in the absence of Mn^II, or in the presence of EDTA, exhibited diminished electron density at this site. Crystals grown in excess Mn^II exhibited increased electron density at the proposed binding site but nowhere else in the protein. This suggests that there is only one major Mn^II binding site in MnP. Crystal structures of a single mutant (D179N) and a double mutant (E35Q,D179N) at this site were determined. The mutant structures lack a cation at the Mn^II binding site. The structure of the Mn^II binding site is altered significantly in both mutants, resulting in increased access to the solvent and substrate.

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