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

Toshitaka Matsui, Shusuke Nambu, Yukari Ono, Celia W. Goulding, Kouhei Tsumoto, Masao Ikeda-Saito

Research output: Contribution to journalArticlepeer-review

61 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3025-3027
Number of pages3
JournalBiochemistry
Volume52
Issue number18
DOIs
Publication statusPublished - 2013 May 7

ASJC Scopus subject areas

  • Biochemistry

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