PMID:8253713
| Citation |
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 |
|---|---|
| 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 | |
| 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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