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Science 21 August 1998: Vol. 281. no. 5380, pp. 1197 - 1200 DOI: 10.1126/science.281.5380.1197
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Reports
Prototype of a Heme Chaperone Essential for Cytochrome c Maturation
Henk Schulz,
Hauke Hennecke,
Linda Thöny-Meyer
*
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.
Mikrobiologisches Institut, Eidgenössische Technische
Hochschule, Schmelzbergstrasse 7, CH-8092 Zürich, Switzerland.
*
To whom correspondence should be addressed. E-mail:
lthoeny{at}micro.biol.ethz.ch
Read the Full Text
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