Structural and biochemical study of Bacillus subtilis HmoB in complex with heme |
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Authors: | Seonghun Park Dajeong Kim Inae Jang Han Bin Oh Jungwoo Choe |
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Affiliation: | 1. Ildong Pharmaceutical Co., Ltd, Gyeonggi-do 445-170, Republic of Korea;2. Department of Life Science, University of Seoul, Seoul 130-743, Republic of Korea;3. Department of Chemistry, Sogang University, Seoul 121-742, Republic of Korea |
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Abstract: | 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. |
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Keywords: | ABM domain, antibiotic biosynthesis monooxygenase domain RMSD, root-mean-square deviation |
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