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Prototype of a Heme Chaperone Essential for Cytochrome c Maturation

Science  21 Aug 1998:
Vol. 281, Issue 5380, pp. 1197-1200
DOI: 10.1126/science.281.5380.1197

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Abstract

Heme, the iron-containing cofactor essential for the activity of many enzymes, is incorporated into its target proteins by unknown mechanisms. Here, an Escherichia coli hemoprotein, CcmE, was shown to bind heme in the bacterial periplasm by way of a single covalent bond to a histidine. The heme was then released and delivered to apocytochrome c. Thus, CcmE can be viewed as a heme chaperone guiding heme to its appropriate biological partner and preventing illegitimate complex formation.

  • * To whom correspondence should be addressed. E-mail: lthoeny{at}micro.biol.ethz.ch

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