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Applied and Environmental Microbiology, June 2009, p. 4130-4138, Vol. 75, No. 12
0099-2240/09/$08.00+0     doi:10.1128/AEM.02890-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mn(II) Oxidation Is Catalyzed by Heme Peroxidases in "Aurantimonas manganoxydans" Strain SI85-9A1 and Erythrobacter sp. Strain SD-21{triangledown}

C. R. Anderson,1,§,{dagger} H. A. Johnson,2,§ N. Caputo,1 R. E. Davis,1 J. W. Torpey,3 and B. M. Tebo1*

Division of Environmental and Biomolecular Systems, Oregon Health & Science University, 20000 NW Walker Road, Beaverton, Oregon 97006,1 Department of Biological Sciences, California State University, Fullerton, P.O. Box 6850, Fullerton, California 92834-6850,2 Biomolecular Mass Spectrometry Facility, Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, California 92093-03783

Received 18 December 2008/ Accepted 19 April 2009

A new type of manganese-oxidizing enzyme has been identified in two alphaproteobacteria, "Aurantimonas manganoxydans" strain SI85-9A1 and Erythrobacter sp. strain SD-21. These proteins were identified by tandem mass spectrometry of manganese-oxidizing bands visualized by native polyacrylamide gel electrophoresis in-gel activity assays and fast protein liquid chromatography-purified proteins. Proteins of both alphaproteobacteria contain animal heme peroxidase and hemolysin-type calcium binding domains, with the 350-kDa active Mn-oxidizing protein of A. manganoxydans containing stainable heme. The addition of both Ca2+ ions and H2O2 to the enriched protein from Aurantimonas increased manganese oxidation activity 5.9-fold, and the highest activity recorded was 700 µM min–1 mg–1. Mn(II) is oxidized to Mn(IV) via an Mn(III) intermediate, which is consistent with known manganese peroxidase activity in fungi. The Mn-oxidizing protein in Erythrobacter sp. strain SD-21 is 225 kDa and contains only one peroxidase domain with strong homology to the first 2,000 amino acids of the peroxidase protein from A. manganoxydans. The heme peroxidase has tentatively been named MopA (manganese-oxidizing peroxidase) and sheds new light on the molecular mechanism of Mn oxidation in prokaryotes.

* Corresponding author. Mailing address: Division of Environmental and Biomolecular Systems, Oregon Health & Science University, 20000 NW Walker Road, Beaverton, OR 97006. Phone: (503) 748-1992. Fax: (503) 748-1464. E-mail: tebo{at}ebs.ogi.edu

{triangledown} Published ahead of print on 1 May 2009.

§ These authors contributed equally to this work.

{dagger} Present address: Bio-Protection Research Centre, P.O. Box 84, Lincoln University, Lincoln 7647, New Zealand.

Applied and Environmental Microbiology, June 2009, p. 4130-4138, Vol. 75, No. 12
0099-2240/09/$08.00+0     doi:10.1128/AEM.02890-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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