Prototype of a Heme Chaperone Essential for Cytochrome c Maturation
- 21 August 1998
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 281 (5380) , 1197-1200
- https://doi.org/10.1126/science.281.5380.1197
Abstract
Heme, the iron-containing cofactor essential for the activity of many enzymes, is incorporated into its target proteins by unknown mechanisms. Here, anEscherichia colihemoprotein, 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.Keywords
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