PMID:9712585

Citation	Schulz, H, Hennecke, H and Thöny-Meyer, L (1998) Prototype of a heme chaperone essential for cytochrome c maturation. Science 281:1197-200
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.
Links	PubMed
Keywords	Amino Acid Sequence; Apoproteins/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Cytochrome c Group/metabolism; Cytochromes c; Escherichia coli/genetics; Escherichia coli/metabolism; Heme/metabolism; Histidine/metabolism; Mass Spectrometry; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Recombinant Fusion Proteins/metabolism
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