https://ecoliwiki.org/colipedia/api.php?action=feedcontributions&feedformat=atom&user=66.249.70.122EcoliWiki - User contributions [en]2026-11-02T21:14:41ZUser contributionsMediaWiki 1.43.11https://ecoliwiki.org/colipedia/index.php?title=PMID:8253713&diff=95917PMID:82537132007-07-24T00:39:01Z<p>66.249.70.122: New PMID: Page!</p>
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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><br />
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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.<br />
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8253713 PubMed]<br />
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