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Appl Environ Microbiol. 1994 June; 60(6): 1956-1961
Copyright © 1994, American Society for Microbiology. All Rights Reserved.

Lipid Peroxidation by the Manganese Peroxidase of Phanerochaete chrysosporium Is the Basis for Phenanthrene Oxidation by the Intact Fungus

Mark A. Moen and Kenneth E. Hammel*

Institute for Microbial and Biochemical Technology, Forest Products Laboratory, U.S. Department of Agriculture, Madison, Wisconsin 53705

ABSTRACT

The manganese peroxidase (MnP) of Phanerochaete chrysosporium supported Mn(II)-dependent, H2O2-independent lipid peroxidation, as shown by two findings: linolenic acid was peroxidized to give products that reacted with thiobarbituric acid, and linoleic acid was peroxidized to give hexanal. MnP also supported the slow oxidation of phenanthrene to 2,2'-diphenic acid in a reaction that required Mn(II), oxygen, and unsaturated lipids. Phenanthrene oxidation to diphenic acid by intact cultures of P. chrysosporium occurred to the same extent that oxidation in vitro did and was stimulated by Mn. These results support a role for MnP-mediated lipid peroxidation in phenanthrene oxidation by P. chrysosporium.

FOOTNOTES

* Corresponding author. Mailing address: Forest Products Laboratory, U.S. Department of Agriculture, One Gifford Pinchot Dr., Madison, WI 53705. Fax: (608) 231-9262. Electronic mail address: kehammel@facstaff.wisc.edu.

Appl Environ Microbiol. 1994 June; 60(6): 1956-1961
Copyright © 1994, American Society for Microbiology. All Rights Reserved.



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