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Medientyp:
E-Artikel
Titel:
Prototype of a Heme Chaperone Essential for Cytochrome c Maturation
Beteiligte:
Schulz, Henk;
Hennecke, Hauke;
Thöny-Meyer, Linda
Erschienen:
American Association for the Advancement of Science (AAAS), 1998
Erschienen in:
Science, 281 (1998) 5380, Seite 1197-1200
Sprache:
Englisch
DOI:
10.1126/science.281.5380.1197
ISSN:
0036-8075;
1095-9203
Entstehung:
Anmerkungen:
Beschreibung:
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.