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Biochemistry. 2013 May 7;52(18):3025-7. doi: 10.1021/bi400382p. Epub 2013 Apr 24.

Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide.

Author information

1
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira, Aoba, Sendai 980-8577, Japan.

Abstract

IsdG and IsdI from Staphylococcus aureus are novel heme-degrading enzymes containing unusually nonplanar (ruffled) heme. While canonical heme-degrading enzymes, heme oxygenases, catalyze heme degradation coupled with the release of CO, in this study we demonstrate that the primary C1 product of the S. aureus enzymes is formaldehyde. This finding clearly reveals that both IsdG and IsdI degrade heme by an unusual mechanism distinct from the well-characterized heme oxygenase mechanism as recently proposed for MhuD from Mycobacterium tuberculosis. We conclude that heme ruffling is critical for the drastic mechanistic change for these novel bacterial enzymes.

PMID:
23600533
PMCID:
PMC3672231
DOI:
10.1021/bi400382p
[Indexed for MEDLINE]
Free PMC Article

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