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Bacillus subtilis CtaA is a heme-containing membrane proteininvolved in heme A biosynthesis

Svensson, B. and Hederstedt, Lars LU (1994) In Journal of Bacteriology 176(21). p.6663-6671
Abstract
Heme A is a prosthetic group of many respiratory oxidases. It is synthesized from protoheme IX (heme B) seemingly with heme O as a stable intermediate. The Bacillus subtilis ctaA and ctaB genes are required for heme A and heme O synthesis, respectively (B. Svensson, M. Lubben, and L. Hederstedt, Mol. Microbiol. 10:193-201, 1993). Tentatively, CtaA is involved in the monooxygenation and oxidation of the methyl side group on porphyrin ring D in heme A synthesis from heme B. B. subtilis ctaA and ctaB on plasmids in both B. subtilis and Escherichia coli were found to result in a novel membrane-bound heme-containing protein with the characteristics of a low-spin b type cytochrome. It fan be reduced via the respiratory chain, and in the reduced... (More)
Heme A is a prosthetic group of many respiratory oxidases. It is synthesized from protoheme IX (heme B) seemingly with heme O as a stable intermediate. The Bacillus subtilis ctaA and ctaB genes are required for heme A and heme O synthesis, respectively (B. Svensson, M. Lubben, and L. Hederstedt, Mol. Microbiol. 10:193-201, 1993). Tentatively, CtaA is involved in the monooxygenation and oxidation of the methyl side group on porphyrin ring D in heme A synthesis from heme B. B. subtilis ctaA and ctaB on plasmids in both B. subtilis and Escherichia coli were found to result in a novel membrane-bound heme-containing protein with the characteristics of a low-spin b type cytochrome. It fan be reduced via the respiratory chain, and in the reduced state it shows light absorption maxima at 428, 528, and 558 nm and the or-band is split. Purified cytochrome isolated from both B. subtilis and E. coli membranes contained one polypeptide identified as CtaA by amino acid sequence analysis, about 0.2 mol of heme B per mol of polypeptide, and small amounts of heme A. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Bacteriology
volume
176
issue
21
pages
6663 - 6671
publisher
American Society for Microbiology
external identifiers
  • scopus:0028046467
ISSN
0021-9193
DOI
10.1128/jb.176.21.6663-6671.1994
language
English
LU publication?
yes
id
44846ede-d441-4e41-b7e9-5579df433b3c
date added to LUP
2017-07-18 10:15:02
date last changed
2017-10-08 05:05:05
@article{44846ede-d441-4e41-b7e9-5579df433b3c,
  abstract     = {Heme A is a prosthetic group of many respiratory oxidases. It is synthesized from protoheme IX (heme B) seemingly with heme O as a stable intermediate. The Bacillus subtilis ctaA and ctaB genes are required for heme A and heme O synthesis, respectively (B. Svensson, M. Lubben, and L. Hederstedt, Mol. Microbiol. 10:193-201, 1993). Tentatively, CtaA is involved in the monooxygenation and oxidation of the methyl side group on porphyrin ring D in heme A synthesis from heme B. B. subtilis ctaA and ctaB on plasmids in both B. subtilis and Escherichia coli were found to result in a novel membrane-bound heme-containing protein with the characteristics of a low-spin b type cytochrome. It fan be reduced via the respiratory chain, and in the reduced state it shows light absorption maxima at 428, 528, and 558 nm and the or-band is split. Purified cytochrome isolated from both B. subtilis and E. coli membranes contained one polypeptide identified as CtaA by amino acid sequence analysis, about 0.2 mol of heme B per mol of polypeptide, and small amounts of heme A.},
  author       = {Svensson, B. and Hederstedt, Lars},
  issn         = {0021-9193},
  language     = {eng},
  number       = {21},
  pages        = {6663--6671},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {<em>Bacillus subtilis</em> CtaA is a heme-containing membrane proteininvolved in heme A biosynthesis},
  url          = {http://dx.doi.org/10.1128/jb.176.21.6663-6671.1994 },
  volume       = {176},
  year         = {1994},
}