Prototype of a Heme Chaperone Essential for Cytochrome c Maturation
1998; American Association for the Advancement of Science; Volume: 281; Issue: 5380 Linguagem: Inglês
10.1126/science.281.5380.1197
ISSN1095-9203
AutoresHenk Schulz, Hauke Hennecke, Linda Thöny‐Meyer,
Tópico(s)RNA and protein synthesis mechanisms
ResumoHeme, 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.
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