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- Title
Prototype of a heme chaperone essential for cytochrome c maturation.
- Authors
Schulz, H; Hennecke, H; Thöny-Meyer, L
- 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.
- Publication
Science (New York, N.Y.), 1998, Vol 281, Issue 5380, p1197
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.281.5380.1197