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J. Biol. Chem., Vol. 279, Issue 44, 45791-45802, October 29, 2004

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The Heme Oxygenase(s)-Phytochrome System of Pseudomonas aeruginosa^*

Rosalina Wegele, Ronja Tasler, Yuhong Zeng, Mario Rivera, and Nicole Frankenberg-Dinkel¶

From the Institute for Microbiology, Technical University Braunschweig, Spielmannstrasse 7, 38106 Braunschweig, Germany and the Department of Chemistry, University of Kansas, Lawrence, Kansas 66045-7582

For many pathogenic bacteria like Pseudomonas aeruginosa heme is an essential source of iron. After uptake, the heme molecule is degraded by heme oxygenases to yield iron, carbon monoxide, and biliverdin. The heme oxygenase PigA is only induced under iron-limiting conditions and produces the unusual biliverdin isomers IX and IX. The gene for a second putative heme oxygenase in P. aeruginosa, bphO, occurs in an operon with the gene bphP encoding a bacterial phytochrome. Here we provide biochemical evidence that bphO encodes for a second heme oxygenase in P. aeruginosa. HPLC, ¹H, and ¹³C NMR studies indicate that BphO is a "classic" heme oxygenase in that it produces biliverdin IX. The data also suggest that the overall fold of BphO is likely to be the same as that reported for other -hydroxylating heme oxygenases. Recombinant BphO was shown to prefer ferredoxins or ascorbate as a source of reducing equivalents in vitro and the rate-limiting step for the oxidation of heme to biliverdin is the release of product. In eukaryotes, the release of biliverdin is driven by biliverdin reductase, the subsequent enzyme in heme catabolism. Because P. aeruginosa lacks a biliverdin reductase homologue, data are presented indicating an involvement of the bacterial phytochrome BphP in biliverdin release from BphO and possibly from PigA.

Received for publication, July 22, 2004 , and in revised form, August 11, 2004.

^* This work was supported by the Emmy-Noether-Program of the Deutsche Forschungsgemeinschaft and funds from the Fonds der Chemischen Industrie (to N. F.-D.) and by Grant GM 50503 from the National Institutes of Health (to M. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Tel.: 49-531-391-5815; Fax: 49-531-391-5854; E-mail: n.frankenberg{at}tu-bs.de.

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