TITLE

Over-Expression and Characterization of Bacillus subtilis Heme O Synthase

AUTHOR(S)
Mogi, Tatsushi
PUB. DATE
May 2009
SOURCE
Journal of Biochemistry;May2009, Vol. 145 Issue 5, p669
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Biosynthesis of heme A from heme B is catalysed by two enzymes, heme O and heme A synthases, in the membrane. Heme O synthase in Bacillus subtilis (CtaB) has eight transmembrane helices and catalyses 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 extra-cellular 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.
ACCESSION #
44544306

 

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