Prototype of a heme chaperone essential for cytochrome c maturation.
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.
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Schulz
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Hennecke
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Thöny-Meyer
D000595:Amino Acid Sequence; D001059:Apoproteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D003574:Cytochrome c Group / Q000378:metabolism*; D045304:Cytochromes c; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D001059:Apoproteins; D001426:Bacterial Proteins; D003574:Cytochrome c Group; D008565:Membrane Proteins; D018832:Molecular Chaperones; D011993:Recombinant Fusion Proteins; D006418:Heme; D006639:Histidine; D045304:Cytochromes c