Expression of prokaryotic and eukaryotic cytochromes c in Escherichia coli

Autor(en): Sanders, C
Lill, H
Stichwörter: BACTERIA; Biochemistry & Molecular Biology; BIOGENESIS; Biophysics; ccm system; CHLOROPLASTS; cytochrome c; Escherichia coli; GENE; heme attachment; heme lyase; heterologous expression; IDENTIFICATION; LOCUS; MATURATION; OXIDASE; SEQUENCE; YEAST SACCHAROMYCES-CEREVISIAE
Erscheinungsdatum: 2000
Herausgeber: ELSEVIER SCIENCE BV
Journal: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volumen: 1459
Ausgabe: 1
Startseite: 131
Seitenende: 138
Zusammenfassung: 
C-type cytochromes from various sources show substantial structural conservation. For the covalent attachment of heme groups to apocytochromes, however, three different enzyme systems have been described so far. We have examined the ability of the heme ligation systems of Escherichia coli and of Saccharomyces cerevisiae to process cytochromes from S. cerevisiae, Paracoccus denitrificans, and Synechocystis sp. PCC 6803. E. coli's maturation system with at least eight different proteins accepted all these cytochromes for heme ligation. The single subunit heme lyase from S. cerevisiae mitochondria, on the other hand, failed to attach heme groups to cytochromes of prokaryotic origin. (C) 2000 Elsevier Science B.V. All rights reserved.
ISSN: 00052728
DOI: 10.1016/S0005-2728(00)00122-5

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