Structural and biochemical study of Bacillus subtilis HmoB in complex with heme

Seonghun Park, Dajeong Kim, Inae Jang, Han Bin Oh, Jungwoo Choe

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10 Scopus citations


Most bacteria have developed a hemoprotein degradation system to acquire iron from their hosts. Bacillus subtilis HmoB, a heme monooxygenase, is involved in the degradation of heme and subsequent release of iron. HmoB contains a C-terminal ABM domain, which is similar in sequence and structure to other heme monooxygenases. Heme degradation assay showed that highly conserved residues (N70, W128, and H138) near the heme-binding site were critical for activity of HmoB. However, HmoB was shown to be different from other bacterial heme oxygenases due to its longer N-terminal region and formation of a biological monomer instead of a dimer. The degradation product of B. subtilis HmoB was identified as staphylobilin from mass spectrometric analysis of the product and release of formaldehyde during degradation reaction.

Original languageEnglish
Pages (from-to)286-291
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 28 Mar 2014


  • ABM domain
  • Crystallography
  • Heme degradation
  • Heme monooxygenase
  • Iron


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