Abstract:
:Heme A, as a prosthetic group, is found exclusively in respiratory oxidases of mitochondria and aerobic bacteria. Bacillus subtilis CtaA and other heme A synthases catalyze the conversion of a methyl side group on heme O into a formyl group. The catalytic mechanism of heme A synthase is not understood, and little is known about the composition and structure of the enzyme. In this work, we have: (i) constructed a ctaA deletion mutant and a system for overproduction of mutant variants of the CtaA protein in B. subtilis, (ii) developed anaffinity purification procedure for isolation of preparative amounts of CtaA, and (iii) investigated the functional roles of four invariant histidine residues in heme A synthase by in vivo and in vitro analyses of the properties of mutant variants of CtaA. Our results show an important function of three histidine residues for heme A synthase activity. Several of the purified mutant enzyme proteins contained tightly bound heme O. One variant also contained trapped hydroxylated heme O, which is a postulated enzyme reaction intermediate. The findings indicate functional roles for the invariant histidine residues and provide strong evidence that the heme A synthase enzyme reaction includes two consecutive monooxygenations.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Hederstedt L,Lewin A,Throne-Holst Mdoi
10.1128/JB.187.24.8361-8369.2005keywords:
subject
Has Abstractpub_date
2005-12-01 00:00:00pages
8361-9issue
24eissn
0021-9193issn
1098-5530pii
187/24/8361journal_volume
187pub_type
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journal_title:Journal of bacteriology
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