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Bioinformatic analyses of the<jats:italic>B. anthracis<\/jats:italic>genome revealed genes with similarity to the<jats:italic>i<\/jats:italic>ron-regulated<jats:italic>s<\/jats:italic>urface<jats:italic>d<\/jats:italic>eterminant (<jats:italic>isd<\/jats:italic>) system responsible for heme uptake in<jats:italic>Staphylococcus aureus<\/jats:italic>. We show that the protein product of one of these genes,<jats:italic>isdG<\/jats:italic>, binds hemin in a manner resembling the heme binding of known heme oxygenases. Formation of IsdG:hemin complexes in the presence of a suitable electron donor, e.g., ascorbate or cytochrome P450 reductase, promotes catalytic degradation of hemin to biliverdin with concomitant release of iron. IsdG is required for<jats:italic>B. anthracis<\/jats:italic>utilization of hemin as a sole iron source, and it is also necessary for bacterial protection against heme-mediated toxicity. 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