PMID:16428411

Citation	Skaar, EP, Gaspar, AH and Schneewind, O (2006) Bacillus anthracis IsdG, a heme-degrading monooxygenase. J. Bacteriol. 188:1071-80
Abstract	Bacillus anthracis, the causative agent of anthrax, utilizes hemin and hemoglobin for growth in culture, suggesting that these host molecules serve as sources for the nutrient iron during bacterial infection. Bioinformatic analyses of the B. anthracis genome revealed genes with similarity to the iron-regulated surface determinant (isd) system responsible for heme uptake in Staphylococcus aureus. We show that the protein product of one of these genes, isdG, 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 B. anthracis utilization of hemin as a sole iron source, and it is also necessary for bacterial protection against heme-mediated toxicity. These data suggest that IsdG functions as a heme-degrading monooxygenase in B. anthracis.
Links	PubMed PMC1347327 Online version:10.1128/JB.188.3.1071-1080.2006
Keywords	Amino Acid Sequence; Bacillus anthracis/enzymology; Bacillus anthracis/genetics; Heme/metabolism; Heme Oxygenase (Decyclizing)/genetics; Heme Oxygenase (Decyclizing)/isolation & purification; Heme Oxygenase (Decyclizing)/metabolism; Iron/metabolism; Molecular Sequence Data; Oxygenases/isolation & purification; Oxygenases/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACAN:ISDG		GO:0006787: porphyrin catabolic process	ECO:0000314:		P		Fig 3A and B	complete
BACAN:ISDG		GO:0009636: response to toxin	ECO:0000315:		P		See Fig 6	complete

References

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