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Enzymology and Protein Engineering

Extracellular Heme Peroxidases in Actinomycetes: a Case of Mistaken Identity

Maria G. Mason, Andrew S. Ball, Brandon J. Reeder, Gary Silkstone, Peter Nicholls, Michael T. Wilson
Maria G. Mason
Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
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Andrew S. Ball
Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
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Brandon J. Reeder
Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
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Gary Silkstone
Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
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Peter Nicholls
Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
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Michael T. Wilson
Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
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DOI: 10.1128/AEM.67.10.4512-4519.2001
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ABSTRACT

Actinomycetes secrete into their surroundings a suite of enzymes involved in the biodegradation of plant lignocellulose; these have been reported to include both hydrolytic and oxidative enzymes, including peroxidases. Reports of secreted peroxidases have been based upon observations of peroxidase-like activity associated with fractions that exhibit optical spectra reminiscent of heme peroxidases, such as the lignin peroxidases of wood-rotting fungi. Here we show that the appearance of the secreted pseudoperoxidase of the thermophilic actinomycete Thermomonospora fusca BD25 is also associated with the appearance of a heme-like spectrum. The species responsible for this spectrum is a metalloporphyrin; however, we show that this metalloporphyrin is not heme but zinc coproporphyrin. The same porphyrin was found in the growth medium of the actinomyceteStreptomyces viridosporus T7A. We therefore propose that earlier reports of heme peroxidases secreted by actinomycetes were due to the incorrect assignment of optical spectra to heme groups rather than to non-iron-containing porphyrins and that lignin-degrading heme peroxidases are not secreted by actinomycetes. The porphyrin, an excretory product, is degraded during peroxidase assays. The low levels of secreted peroxidase activity are associated with a nonheme protein fraction previously shown to contain copper. We suggest that the role of the secreted copper-containing protein may be to bind and detoxify metals that can cause inhibition of heme biosynthesis and thus stimulate porphyrin excretion.

  • Copyright © 2001 American Society for Microbiology
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Extracellular Heme Peroxidases in Actinomycetes: a Case of Mistaken Identity
Maria G. Mason, Andrew S. Ball, Brandon J. Reeder, Gary Silkstone, Peter Nicholls, Michael T. Wilson
Applied and Environmental Microbiology Oct 2001, 67 (10) 4512-4519; DOI: 10.1128/AEM.67.10.4512-4519.2001

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Extracellular Heme Peroxidases in Actinomycetes: a Case of Mistaken Identity
Maria G. Mason, Andrew S. Ball, Brandon J. Reeder, Gary Silkstone, Peter Nicholls, Michael T. Wilson
Applied and Environmental Microbiology Oct 2001, 67 (10) 4512-4519; DOI: 10.1128/AEM.67.10.4512-4519.2001
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KEYWORDS

Actinomycetales
Coproporphyrins
Heme
peroxidases

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