PMID:8253713: Difference between revisions

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<span style = 'font-size: large'> '''Saiki, K, Mogi, T, Ogura, K and Anraku, Y'''  (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli.''J. Biol. Chem.'' '''268''':26041-4</span>
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!align=left  |Citation
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'''No author listed'''  (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli. ''J. Biol. Chem.'' '''268''':26041-4
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!align=left  |Abstract
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The cytochrome bo complex is a heme-copper terminal quinol oxidase in the aerobic respiratory chain of Escherichia coli and contains low spin heme B, high spin heme O and CuB as the redox metal centers in subunit I. Based on site-directed mutagenesis studies on the cyoE gene in the cytochrome bo operon, we have postulated that the cyoE gene encodes a protoheme IX farnesyltransferase (heme O synthase) (Saiki, K., Mogi, T., and Anraku, Y. (1992) Biochem. Biophys. Res. Commun. 189, 1491-1497). The present study demonstrates that the CyoE protein is localized in the cytoplasmic membrane and that the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme IX and farnesyl diphosphate to heme O in the presence of divalent cations such as Mg2+ or Ca2+. Thus, the cyoABCDE operon in E. coli encodes not only subunits of the cytochrome bo complex but also heme O synthase that is specifically required for functional expression of the bo-type quinol oxidase. Heme O seems to be an intermediate in heme A biosynthesis.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8253713 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || The cytochrome bo complex is a heme-copper terminal quinol oxidase in the aerobic respiratory chain of Escherichia coli and contains low spin heme B, high spin heme O and CuB as the redox metal centers in subunit I. Based on site-directed mutagenesis studies on the cyoE gene in the cytochrome bo operon, we have postulated that the cyoE gene encodes a protoheme IX farnesyltransferase (heme O synthase) (Saiki, K., Mogi, T., and Anraku, Y. (1992) Biochem. Biophys. Res. Commun. 189, 1491-1497). The present study demonstrates that the CyoE protein is localized in the cytoplasmic membrane and that the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme IX and farnesyl diphosphate to heme O in the presence of divalent cations such as Mg2+ or Ca2+. Thus, the cyoABCDE operon in E. coli encodes not only subunits of the cytochrome bo complex but also heme O synthase that is specifically required for functional expression of the bo-type quinol oxidase. Heme O seems to be an intermediate in heme A biosynthesis.
!align=left  |Keywords
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Alkyl and Aryl Transferases; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cytochrome b Group; Cytochromes/genetics; Cytochromes/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Ferrochelatase/genetics; Ferrochelatase/metabolism; Heme/biosynthesis
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8253713 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:44, 1 September 2013

Citation

No author listed (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli. J. Biol. Chem. 268:26041-4

Abstract

The cytochrome bo complex is a heme-copper terminal quinol oxidase in the aerobic respiratory chain of Escherichia coli and contains low spin heme B, high spin heme O and CuB as the redox metal centers in subunit I. Based on site-directed mutagenesis studies on the cyoE gene in the cytochrome bo operon, we have postulated that the cyoE gene encodes a protoheme IX farnesyltransferase (heme O synthase) (Saiki, K., Mogi, T., and Anraku, Y. (1992) Biochem. Biophys. Res. Commun. 189, 1491-1497). The present study demonstrates that the CyoE protein is localized in the cytoplasmic membrane and that the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme IX and farnesyl diphosphate to heme O in the presence of divalent cations such as Mg2+ or Ca2+. Thus, the cyoABCDE operon in E. coli encodes not only subunits of the cytochrome bo complex but also heme O synthase that is specifically required for functional expression of the bo-type quinol oxidase. Heme O seems to be an intermediate in heme A biosynthesis.

Links

PubMed

Keywords

Alkyl and Aryl Transferases; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cytochrome b Group; Cytochromes/genetics; Cytochromes/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Ferrochelatase/genetics; Ferrochelatase/metabolism; Heme/biosynthesis

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