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Journal of Biochemistry Advance Access published online on February 9, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp024
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Overexpression and Characterization of Bacillus subtilis Heme O Synthase

Tatsushi Mogi1,2,*

1Department of Biomedical Chemistry, Graduate School of Medicine, the University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033; 2ATP System Project, ERATO, JST, Nagatsuta, Midori-ku, Yokohama 226-0026, Japan

*To whom correspondence addressed. Tel: +81-3-5841-8202, Fax: +81-3-5841-3444, E-mail: tmogi{at}m.u-tokyo.ac.jp.

Received December 20, 2008; Accepted January 31, 2009


  Abstract

Biosynthesis of heme A from heme B is catalyzed by two enzymes, heme O and heme A synthase, in the membrane. Heme O synthase in Bacillus subtilis (CtaB) has eight transmembrane helices and catalyzes the transfer of a farnesyl group from farnesyl diphosphate to the 2-vinyl group on pyrrole ring A of ferrous heme B. In this study, we constructed the overproduction system for the B. subtilis CtaB in Escherichia coli. We isolated His7-CtaB by affinity chromatography and demonstrated the presence of the heme-binding site in heme O synthase. His7-CtaB binds substoichiometric amounts of heme B and O, substrate and unreleased product, respectively. Mutagenesis studies suggest that strictly conserved His199 present at the extracellular side of helix 5 would serve as the heme-binding site. We are hoping that the overproducing system for heme O synthase would help understanding of detailed mechanism on heme O biosynthesis and X-ray crystallographic studies.


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